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Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein)

 DLDH_HUMAN              Reviewed;         509 AA.
P09622; B2R5X0; B4DHG0; B4DT69; Q14131; Q14167; Q59EV8; Q8WTS4;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
25-OCT-2017, entry version 217.
RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
EC=1.8.1.4 {ECO:0000269|PubMed:15712224, ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:16770810, ECO:0000269|PubMed:17404228, ECO:0000269|PubMed:20160912, ECO:0000269|PubMed:20385101};
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=Glycine cleavage system L protein;
Flags: Precursor;
Name=DLD; Synonyms=GCSL, LAD, PHE3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-104.
PubMed=3693355;
Otulakowski G., Robinson B.H.;
"Isolation and sequence determination of cDNA clones for porcine and
human lipoamide dehydrogenase. Homology to other disulfide
oxidoreductases.";
J. Biol. Chem. 262:17313-17318(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3278312; DOI=10.1073/pnas.85.5.1422;
Pons G., Raefsky-Estrin C., Carothers D.J., Pepin R.A., Javed A.A.,
Jesse B.W., Ganapathi M.K., Samols D., Patel M.S.;
"Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase
component human alpha-ketoacid dehydrogenase complexes.";
Proc. Natl. Acad. Sci. U.S.A. 85:1422-1426(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-104.
TISSUE=Liver;
PubMed=8406489; DOI=10.1006/geno.1993.1335;
Feigenbaum A.S., Robinson B.H.;
"The structure of the human dihydrolipoamide dehydrogenase gene (DLD)
and its upstream elements.";
Genomics 17:376-381(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, Brain cortex, and Pericardium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
PubMed=1332063; DOI=10.1073/pnas.89.22.10964;
Johanning G.L., Morris J.I., Madhusudhan K.T., Samols D., Patel M.S.;
"Characterization of the transcriptional regulatory region of the
human dihydrolipoamide dehydrogenase gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:10964-10968(1992).
[11]
SUBUNIT.
PubMed=14638692; DOI=10.1074/jbc.M308172200;
Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
"Organization of the cores of the mammalian pyruvate dehydrogenase
complex formed by E2 and E2 plus the E3-binding protein and their
capacities to bind the E1 and E3 components.";
J. Biol. Chem. 279:6921-6933(2004).
[12]
SUBCELLULAR LOCATION.
PubMed=15888450; DOI=10.1074/jbc.M500310200;
Mitra K., Rangaraj N., Shivaji S.;
"Novelty of the pyruvate metabolic enzyme dihydrolipoamide
dehydrogenase in spermatozoa: correlation of its localization,
tyrosine phosphorylation, and activity during sperm capacitation.";
J. Biol. Chem. 280:25743-25753(2005).
[13]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, CHARACTERIZATION OF
VARIANT DLDD ASP-479, AND MUTAGENESIS OF GLU-466; HIS-485 AND SER-491.
PubMed=17404228; DOI=10.1073/pnas.0610618104;
Babady N.E., Pang Y.P., Elpeleg O., Isaya G.;
"Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 104:6158-6163(2007).
[14]
CATALYTIC ACTIVITY, INTERACTION WITH PDHX, MUTAGENESIS OF LYS-89;
ARG-482; GLU-492 AND LYS-505, AND CHARACTERIZATION OF VARIANTS DLDD
GLU-72; LYS-375; LEU-488 AND GLY-495.
PubMed=20160912; DOI=10.1016/j.molcatb.2009.05.001;
Patel M.S., Korotchkina L.G., Sidhu S.;
"Interaction of E1 and E3 components with the core proteins of the
human pyruvate dehydrogenase complex.";
J. Mol. Catal., B Enzym. 61:2-6(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-143; LYS-410 AND LYS-417,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
CATALYTIC ACTIVITY, INTERACTION WITH PDHX, AND MUTAGENESIS OF HIS-383;
ASP-448; TYR-473 AND ARG-482.
PubMed=20385101; DOI=10.1016/j.bbrc.2010.04.038;
Park Y.H., Patel M.S.;
"Characterization of interactions of dihydrolipoamide dehydrogenase
with its binding protein in the human pyruvate dehydrogenase
complex.";
Biochem. Biophys. Res. Commun. 395:416-419(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER TYR-35, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 36-509 IN COMPLEXES WITH NAD
AND FAD, AND SUBUNIT.
PubMed=15946682; DOI=10.1016/j.jmb.2005.05.014;
Brautigam C.A., Chuang J.L., Tomchick D.R., Machius M., Chuang D.T.;
"Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH
binding and the structural basis of disease-causing mutations.";
J. Mol. Biol. 350:543-552(2005).
[23]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 36-509.
PubMed=16263718; DOI=10.1074/jbc.M507850200;
Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K.,
Korotchkina L.G., Patel M.S.;
"How dihydrolipoamide dehydrogenase-binding protein binds
dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase
complex.";
J. Biol. Chem. 281:648-655(2006).
[24]
X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 36-509 IN COMPLEX WITH PDHX,
CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT DLDD GLY-495.
PubMed=16442803; DOI=10.1016/j.str.2006.01.001;
Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R.,
Chuang D.T.;
"Structural insight into interactions between dihydrolipoamide
dehydrogenase (E3) and E3 binding protein of human pyruvate
dehydrogenase complex.";
Structure 14:611-621(2006).
[25]
CRYO-ELECTRON MICROSCOPY (33.3 ANGSTROMS) OF INNER CORE OF THE
COMPLEX, AND SUBUNIT.
PubMed=20361979; DOI=10.1016/j.jmb.2010.03.043;
Vijayakrishnan S., Kelly S.M., Gilbert R.J., Callow P., Bhella D.,
Forsyth T., Lindsay J.G., Byron O.;
"Solution structure and characterisation of the human pyruvate
dehydrogenase complex core assembly.";
J. Mol. Biol. 399:71-93(2010).
[26]
VARIANTS DLDD GLU-72 AND LEU-488.
PubMed=8506365; DOI=10.1073/pnas.90.11.5186;
Liu T.-C., Kim H., Arizmendi C., Kitano A., Patel M.S.;
"Identification of two missense mutations in a dihydrolipoamide
dehydrogenase-deficient patient.";
Proc. Natl. Acad. Sci. U.S.A. 90:5186-5190(1993).
[27]
VARIANTS DLDD GLY-136 DEL AND LYS-375.
PubMed=9540846; DOI=10.1016/S0925-4439(97)00073-2;
Hong Y.S., Kerr D.S., Liu T.C., Lusk M., Powell B.R., Patel M.S.;
"Deficiency of dihydrolipoamide dehydrogenase due to two mutant
alleles (E340K and G101del). Analysis of a family and prenatal
testing.";
Biochim. Biophys. Acta 1362:160-168(1997).
[28]
VARIANT DLDD GLY-495.
PubMed=8968745; DOI=10.1093/hmg/5.12.1925;
Hong Y.S., Kerr D.S., Craigen W.J., Tan J., Pan Y., Lusk M.,
Patel M.S.;
"Identification of two mutations in a compound heterozygous child with
dihydrolipoamide dehydrogenase deficiency.";
Hum. Mol. Genet. 5:1925-1930(1996).
[29]
VARIANT DLDD VAL-479.
PubMed=10448086; DOI=10.1006/bbrc.1999.1133;
Shany E., Saada A., Landau D., Shaag A., Hershkovitz E., Elpeleg O.N.;
"Lipoamide dehydrogenase deficiency due to a novel mutation in the
interface domain.";
Biochem. Biophys. Res. Commun. 262:163-166(1999).
[30]
VARIANTS DLDD VAL-361 AND LYS-375.
PubMed=11687750;
Cerna L., Wenchich L., Hansikova H., Kmoch S., Peskova K.,
Chrastina P., Brynda J., Zeman J.;
"Novel mutations in a boy with dihydrolipoamide dehydrogenase
deficiency.";
Med. Sci. Monit. 7:1319-1325(2001).
[31]
VARIANT DLDD THR-393.
PubMed=12925875; DOI=10.1007/s00431-003-1282-z;
Grafakou O., Oexle K., van den Heuvel L., Smeets R., Trijbels F.,
Goebel H.H., Bosshard N., Superti-Furga A., Steinmann B., Smeitink J.;
"Leigh syndrome due to compound heterozygosity of dihydrolipoamide
dehydrogenase gene mutations. Description of the first E3 splice site
mutation.";
Eur. J. Pediatr. 162:714-718(2003).
[32]
VARIANT DLDD GLY-482, CHARACTERIZATION OF VARIANT DLDD GLY-482, AND
CATALYTIC ACTIVITY.
PubMed=15712224; DOI=10.1002/humu.9319;
Odievre M.H., Chretien D., Munnich A., Robinson B.H., Dumoulin R.,
Masmoudi S., Kadhom N., Roetig A., Rustin P., Bonnefont J.P.;
"A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit
gene (DLD) resulting in an atypical form of alpha-ketoglutarate
dehydrogenase deficiency.";
Hum. Mutat. 25:323-324(2005).
[33]
VARIANTS DLDD THR-47; CYS-229 AND LYS-375, AND CATALYTIC ACTIVITY.
PubMed=16770810; DOI=10.1002/ajmg.a.31313;
Cameron J.M., Levandovskiy V., Mackay N., Raiman J., Renaud D.L.,
Clarke J.T., Feigenbaum A., Elpeleg O., Robinson B.H.;
"Novel mutations in dihydrolipoamide dehydrogenase deficiency in two
cousins with borderline-normal PDH complex activity.";
Am. J. Med. Genet. A 140:1542-1552(2006).
[34]
VARIANT DLDD CYS-229.
PubMed=9934985;
DOI=10.1002/(SICI)1096-8628(19990115)82:2<177::AID-AJMG15>3.0.CO;2-9;
Shaag A., Saada A., Berger I., Mandel H., Joseph A., Feigenbaum A.,
Elpeleg O.N.;
"Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi
Jews.";
Am. J. Med. Genet. 82:177-182(1999).
-!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
cleavage system as well as an E3 component of three alpha-ketoacid
dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and
branched-chain amino acid-dehydrogenase complex). In monomeric
form has additional moonlighting function as serine protease
(PubMed:17404228). Involved in the hyperactivation of spermatazoa
during capacitation and in the spermatazoal acrosome reaction (By
similarity). {ECO:0000250|UniProtKB:Q811C4,
ECO:0000269|PubMed:17404228}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH. {ECO:0000269|PubMed:15712224,
ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:16770810,
ECO:0000269|PubMed:17404228, ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:20385101}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15946682,
ECO:0000269|PubMed:16442803};
Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15946682,
ECO:0000269|PubMed:16442803};
-!- ENZYME REGULATION: Disruption of native heterodimer state inhibits
primary dihydrolipoamide dehydrogenase activity and induces serine
protease activity. {ECO:0000269|PubMed:17404228}.
-!- SUBUNIT: Homodimer (PubMed:15946682). Part of the multimeric
pyruvate dehydrogenase complex that contains multiple copies of
pyruvate dehydrogenase (subunits PDH1A and PDHB, E1),
dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide
dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are
bound to an inner core composed of about 48 DLAT and 12 PDHX
molecules (by non covalent bonds) (PubMed:14638692,
PubMed:20361979). Interacts with PDHX (PubMed:20385101,
PubMed:16442803, PubMed:20160912, PubMed:20361979).
{ECO:0000269|PubMed:14638692, ECO:0000269|PubMed:15946682,
ECO:0000269|PubMed:16442803, ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:20361979, ECO:0000269|PubMed:20385101}.
-!- INTERACTION:
O00330:PDHX; NbExp=3; IntAct=EBI-353366, EBI-751566;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000305|PubMed:3693355}. Cytoplasmic vesicle, secretory
vesicle, acrosome {ECO:0000269|PubMed:15888450}. Cell projection,
cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P09622-1; Sequence=Displayed;
Name=2;
IsoId=P09622-2; Sequence=VSP_055855;
Note=No experimental confirmation available.;
Name=3;
IsoId=P09622-3; Sequence=VSP_055856;
Note=No experimental confirmation available.;
-!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
-!- DISEASE: Dihydrolipoamide dehydrogenase deficiency (DLDD)
[MIM:246900]: An autosomal recessive metabolic disorder
characterized biochemically by a combined deficiency of the
branched-chain alpha-keto acid dehydrogenase complex (BCKDC),
pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate
dehydrogenase complex (KGDC). Clinically, affected individuals
have lactic acidosis and neurologic deterioration due to
sensitivity of the central nervous system to defects in oxidative
metabolism. {ECO:0000269|PubMed:10448086,
ECO:0000269|PubMed:11687750, ECO:0000269|PubMed:12925875,
ECO:0000269|PubMed:15712224, ECO:0000269|PubMed:16442803,
ECO:0000269|PubMed:16770810, ECO:0000269|PubMed:17404228,
ECO:0000269|PubMed:20160912, ECO:0000269|PubMed:8506365,
ECO:0000269|PubMed:8968745, ECO:0000269|PubMed:9540846,
ECO:0000269|PubMed:9934985}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92940.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J03490; AAA59527.1; -; mRNA.
EMBL; J03620; AAA35764.1; -; mRNA.
EMBL; L13761; AAB01381.1; -; Genomic_DNA.
EMBL; L13749; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13750; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13751; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13752; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13753; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13754; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13748; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13755; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13759; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13760; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13756; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13757; AAB01381.1; JOINED; Genomic_DNA.
EMBL; L13758; AAB01381.1; JOINED; Genomic_DNA.
EMBL; AK295080; BAG58122.1; -; mRNA.
EMBL; AK300077; BAG61881.1; -; mRNA.
EMBL; AK312346; BAG35267.1; -; mRNA.
EMBL; AB209703; BAD92940.1; ALT_INIT; mRNA.
EMBL; AC005046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236947; EAL24389.1; -; Genomic_DNA.
EMBL; CH471070; EAW83421.1; -; Genomic_DNA.
EMBL; BC018648; AAH18648.1; -; mRNA.
EMBL; BC018696; AAH18696.1; -; mRNA.
EMBL; M99384; AAA35759.1; -; Genomic_DNA.
CCDS; CCDS5749.1; -. [P09622-1]
CCDS; CCDS78268.1; -. [P09622-3]
PIR; A92622; DEHULP.
RefSeq; NP_000099.2; NM_000108.4. [P09622-1]
RefSeq; NP_001276679.1; NM_001289750.1. [P09622-2]
RefSeq; NP_001276680.1; NM_001289751.1.
RefSeq; NP_001276681.1; NM_001289752.1. [P09622-3]
UniGene; Hs.131711; -.
PDB; 1ZMC; X-ray; 2.53 A; A/B/C/D/E/F/G/H=36-509.
PDB; 1ZMD; X-ray; 2.08 A; A/B/C/D/E/F/G/H=36-509.
PDB; 1ZY8; X-ray; 2.59 A; A/B/C/D/E/F/G/H/I/J=36-509.
PDB; 2F5Z; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/J=36-509.
PDB; 3RNM; X-ray; 2.40 A; A/B/C/D=36-509.
PDBsum; 1ZMC; -.
PDBsum; 1ZMD; -.
PDBsum; 1ZY8; -.
PDBsum; 2F5Z; -.
PDBsum; 3RNM; -.
ProteinModelPortal; P09622; -.
SMR; P09622; -.
BioGrid; 108082; 81.
CORUM; P09622; -.
DIP; DIP-29027N; -.
IntAct; P09622; 15.
MINT; MINT-3007138; -.
STRING; 9606.ENSP00000205402; -.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00157; NADH.
iPTMnet; P09622; -.
PhosphoSitePlus; P09622; -.
SwissPalm; P09622; -.
BioMuta; DLD; -.
DMDM; 269849557; -.
REPRODUCTION-2DPAGE; IPI00015911; -.
UCD-2DPAGE; P09622; -.
EPD; P09622; -.
MaxQB; P09622; -.
PaxDb; P09622; -.
PeptideAtlas; P09622; -.
PRIDE; P09622; -.
DNASU; 1738; -.
Ensembl; ENST00000205402; ENSP00000205402; ENSG00000091140. [P09622-1]
Ensembl; ENST00000417551; ENSP00000390667; ENSG00000091140. [P09622-1]
Ensembl; ENST00000437604; ENSP00000387542; ENSG00000091140. [P09622-3]
GeneID; 1738; -.
KEGG; hsa:1738; -.
UCSC; uc003vet.5; human. [P09622-1]
CTD; 1738; -.
DisGeNET; 1738; -.
EuPathDB; HostDB:ENSG00000091140.12; -.
GeneCards; DLD; -.
H-InvDB; HIX0006994; -.
HGNC; HGNC:2898; DLD.
HPA; HPA044849; -.
MalaCards; DLD; -.
MIM; 238331; gene.
MIM; 246900; phenotype.
neXtProt; NX_P09622; -.
OpenTargets; ENSG00000091140; -.
Orphanet; 2394; Pyruvate dehydrogenase E3 deficiency.
PharmGKB; PA27352; -.
eggNOG; KOG1335; Eukaryota.
eggNOG; COG1249; LUCA.
GeneTree; ENSGT00550000074844; -.
HOGENOM; HOG000276708; -.
HOVERGEN; HBG002290; -.
InParanoid; P09622; -.
KO; K00382; -.
OMA; TMSEAVM; -.
OrthoDB; EOG091G05AA; -.
PhylomeDB; P09622; -.
TreeFam; TF300414; -.
BioCyc; MetaCyc:HS01727-MONOMER; -.
BRENDA; 1.8.1.4; 2681.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-6783984; Glycine degradation.
Reactome; R-HSA-70268; Pyruvate metabolism.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
Reactome; R-HSA-71064; Lysine catabolism.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
SABIO-RK; P09622; -.
ChiTaRS; DLD; human.
EvolutionaryTrace; P09622; -.
GeneWiki; Dihydrolipoamide_dehydrogenase; -.
GenomeRNAi; 1738; -.
PRO; PR:P09622; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000091140; -.
CleanEx; HS_DLD; -.
ExpressionAtlas; P09622; baseline and differential.
Genevisible; P09622; HS.
GO; GO:0043159; C:acrosomal matrix; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:MGI.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; TAS:Reactome.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
GO; GO:0043544; F:lipoamide binding; IEA:Ensembl.
GO; GO:0051287; F:NAD binding; IEA:Ensembl.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0051068; P:dihydrolipoamide metabolic process; IEA:Ensembl.
GO; GO:0007369; P:gastrulation; IEA:Ensembl.
GO; GO:0009106; P:lipoate metabolic process; IEA:Ensembl.
GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IEA:Ensembl.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell projection;
Cilium; Complete proteome; Cytoplasmic vesicle; Disease mutation;
Disulfide bond; FAD; Flagellum; Flavoprotein; Mitochondrion; NAD;
Oxidoreductase; Phosphoprotein; Polymorphism; Redox-active center;
Reference proteome; Transit peptide.
TRANSIT 1 35 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 36 509 Dihydrolipoyl dehydrogenase,
mitochondrial.
/FTId=PRO_0000030295.
NP_BIND 71 80 FAD.
NP_BIND 183 185 FAD.
NP_BIND 220 227 NAD.
NP_BIND 361 364 FAD.
ACT_SITE 487 487 Proton acceptor. {ECO:0000250}.
BINDING 89 89 FAD.
BINDING 154 154 FAD; via amide nitrogen and carbonyl
oxygen.
BINDING 243 243 NAD.
BINDING 278 278 NAD; via amide nitrogen and carbonyl
oxygen.
BINDING 314 314 NAD; via amide nitrogen.
BINDING 355 355 FAD.
SITE 448 448 Important for interaction with PDHX and
activity of multienzyme pyruvate
dehydrogenase complex.
{ECO:0000269|PubMed:20385101}.
SITE 473 473 Important for interaction with PDHX and
activity of multienzyme pyruvate
dehydrogenase complex.
{ECO:0000269|PubMed:20385101}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 104 104 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 104 104 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 122 122 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 132 132 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 132 132 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 143 143 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 143 143 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 159 159 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 166 166 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 273 273 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 277 277 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:Q6P6R2}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 410 410 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 410 410 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 420 420 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 430 430 N6-succinyllysine.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 502 502 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 505 505 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
MOD_RES 505 505 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08749}.
DISULFID 80 85 Redox-active.
VAR_SEQ 1 99 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055855.
VAR_SEQ 147 194 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055856.
VARIANT 47 47 I -> T (in DLDD; dbSNP:rs397514651).
{ECO:0000269|PubMed:16770810}.
/FTId=VAR_076985.
VARIANT 72 72 K -> E (in DLDD; reduced dihydrolipoyl
dehydrogenase activity; no effect on
interaction with PDHX;
dbSNP:rs121964987).
{ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:8506365}.
/FTId=VAR_006907.
VARIANT 104 104 K -> T (in dbSNP:rs1130477).
{ECO:0000269|PubMed:3693355,
ECO:0000269|PubMed:8406489}.
/FTId=VAR_031922.
VARIANT 136 136 Missing (in DLDD).
{ECO:0000269|PubMed:9540846}.
/FTId=VAR_076986.
VARIANT 229 229 G -> C (in DLDD; dbSNP:rs121964990).
{ECO:0000269|PubMed:16770810,
ECO:0000269|PubMed:9934985}.
/FTId=VAR_015820.
VARIANT 331 331 L -> V (in dbSNP:rs17624).
/FTId=VAR_014555.
VARIANT 361 361 M -> V (in DLDD; dbSNP:rs121964993).
{ECO:0000269|PubMed:11687750}.
/FTId=VAR_076987.
VARIANT 375 375 E -> K (in DLDD; loss of enzyme activity;
abolished interaction with PDHX;
dbSNP:rs121964992).
{ECO:0000269|PubMed:11687750,
ECO:0000269|PubMed:16770810,
ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:9540846}.
/FTId=VAR_076988.
VARIANT 393 393 I -> T (in DLDD; dbSNP:rs121964991).
{ECO:0000269|PubMed:12925875}.
/FTId=VAR_076989.
VARIANT 479 479 D -> V (in DLDD; reduced dehydrogenase
activity; increased proteolytic activity;
dbSNP:rs397514649).
{ECO:0000269|PubMed:10448086,
ECO:0000269|PubMed:17404228}.
/FTId=VAR_076990.
VARIANT 482 482 R -> G (in DLDD; reduced enzyme activity;
dbSNP:rs397514650).
/FTId=VAR_076991.
VARIANT 488 488 P -> L (in DLDD; no effect on interaction
with PDHX; dbSNP:rs121964988).
{ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:8506365}.
/FTId=VAR_006908.
VARIANT 495 495 R -> G (in DLDD; loss of enzyme activity;
reduced interaction with PDHX;
dbSNP:rs121964989).
{ECO:0000269|PubMed:16442803,
ECO:0000269|PubMed:20160912,
ECO:0000269|PubMed:8968745}.
/FTId=VAR_015821.
MUTAGEN 89 89 K->E: Abolishes dihydrolipoyl
dehydrogenase activity. Does not affect
interaction with PDHX.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 383 383 H->A: Reduces dihydrolipoyl dehydrogenase
activity. {ECO:0000269|PubMed:20385101}.
MUTAGEN 383 383 H->L: Reduces dihydrolipoyl dehydrogenase
activity. {ECO:0000269|PubMed:20385101}.
MUTAGEN 448 448 D->A: Reduces interaction with PDHX.
Inhibits multienzyme pyruvate
dehydrogenase complex activity. Does not
affect dihydrolipoyl dehydrogenase
activity. {ECO:0000269|PubMed:20385101}.
MUTAGEN 448 448 D->N: Does not affect dihydrolipoyl
dehydrogenase activity.
{ECO:0000269|PubMed:20385101}.
MUTAGEN 466 466 E->A: Decreases dehydrogenase activity.
Loss of proteolytic activity.
{ECO:0000269|PubMed:17404228}.
MUTAGEN 473 473 Y->A: Reduces interaction with PDHX.
Inhibits multienzyme pyruvate
dehydrogenase complex activity. Does not
affect dihydrolipoyl dehydrogenase
activity. {ECO:0000269|PubMed:20385101}.
MUTAGEN 473 473 Y->F: Does not affect dihydrolipoyl
dehydrogenase activity.
{ECO:0000269|PubMed:20385101}.
MUTAGEN 473 473 Y->H: Reduces interaction with PDHX.
Inhibits multienzyme pyruvate
dehydrogenase complex activity. Does not
affect dihydrolipoyl dehydrogenase
activity. {ECO:0000269|PubMed:20385101}.
MUTAGEN 482 482 R->A: Does not affect dihydrolipoyl
dehydrogenase activity.
{ECO:0000269|PubMed:20385101}.
MUTAGEN 482 482 R->M: Does not affect interaction with
PDHX. {ECO:0000269|PubMed:20160912}.
MUTAGEN 485 485 H->A: Loss of dehydrogenase activity.
Increases proteolytic activity.
{ECO:0000269|PubMed:17404228}.
MUTAGEN 491 491 S->A: Loss of proteolytic activity. Does
not affect dehydrogenase activity.
{ECO:0000269|PubMed:17404228}.
MUTAGEN 492 492 E->Q: Reduces dihydrolipoyl dehydrogenase
activity. Does not affect interaction
with PDHX. {ECO:0000269|PubMed:20160912}.
MUTAGEN 505 505 K->M: Reduces dihydrolipoyl dehydrogenase
activity. Does not affect interaction
with PDHX. {ECO:0000269|PubMed:20160912}.
CONFLICT 154 154 G -> R (in Ref. 2; AAA35764).
{ECO:0000305}.
CONFLICT 209 209 L -> F (in Ref. 5; BAD92940).
{ECO:0000305}.
CONFLICT 493 493 A -> AEA (in Ref. 3; AAB01381).
{ECO:0000305}.
STRAND 40 47 {ECO:0000244|PDB:1ZMD}.
HELIX 51 62 {ECO:0000244|PDB:1ZMD}.
STRAND 67 71 {ECO:0000244|PDB:1ZMD}.
STRAND 73 77 {ECO:0000244|PDB:1ZMD}.
HELIX 78 83 {ECO:0000244|PDB:1ZMD}.
HELIX 85 102 {ECO:0000244|PDB:1ZMD}.
HELIX 105 108 {ECO:0000244|PDB:1ZMD}.
STRAND 111 114 {ECO:0000244|PDB:1ZMD}.
STRAND 116 118 {ECO:0000244|PDB:1ZMD}.
HELIX 120 144 {ECO:0000244|PDB:1ZMD}.
STRAND 148 158 {ECO:0000244|PDB:1ZMD}.
STRAND 161 165 {ECO:0000244|PDB:1ZMD}.
STRAND 171 181 {ECO:0000244|PDB:1ZMD}.
STRAND 185 187 {ECO:0000244|PDB:1ZMD}.
STRAND 197 201 {ECO:0000244|PDB:1ZMD}.
HELIX 203 206 {ECO:0000244|PDB:1ZMD}.
STRAND 214 219 {ECO:0000244|PDB:1ZMD}.
HELIX 223 234 {ECO:0000244|PDB:1ZMD}.
STRAND 238 242 {ECO:0000244|PDB:1ZMD}.
STRAND 244 249 {ECO:0000244|PDB:1ZMD}.
HELIX 255 267 {ECO:0000244|PDB:1ZMD}.
STRAND 271 273 {ECO:0000244|PDB:1ZMD}.
STRAND 275 283 {ECO:0000244|PDB:1ZMD}.
STRAND 289 295 {ECO:0000244|PDB:1ZMD}.
STRAND 302 311 {ECO:0000244|PDB:1ZMD}.
STRAND 315 317 {ECO:0000244|PDB:1ZMD}.
HELIX 324 327 {ECO:0000244|PDB:1ZMD}.
STRAND 350 352 {ECO:0000244|PDB:1ZMD}.
HELIX 354 356 {ECO:0000244|PDB:1ZMD}.
STRAND 357 359 {ECO:0000244|PDB:1ZMD}.
HELIX 363 377 {ECO:0000244|PDB:1ZMD}.
HELIX 386 388 {ECO:0000244|PDB:1ZMD}.
STRAND 391 393 {ECO:0000244|PDB:1ZMD}.
STRAND 395 403 {ECO:0000244|PDB:1ZMD}.
HELIX 406 412 {ECO:0000244|PDB:1ZMD}.
STRAND 416 422 {ECO:0000244|PDB:1ZMD}.
HELIX 423 425 {ECO:0000244|PDB:1ZMD}.
HELIX 427 431 {ECO:0000244|PDB:1ZMD}.
STRAND 438 444 {ECO:0000244|PDB:1ZMD}.
TURN 445 447 {ECO:0000244|PDB:1ZMD}.
STRAND 449 457 {ECO:0000244|PDB:1ZMD}.
HELIX 460 473 {ECO:0000244|PDB:1ZMD}.
HELIX 477 482 {ECO:0000244|PDB:1ZMD}.
HELIX 491 503 {ECO:0000244|PDB:1ZMD}.
SEQUENCE 509 AA; 54177 MW; 7613492C516F3835 CRC64;
MQSWSRVYCS LAKRGHFNRI SHGLQGLSAV PLRTYADQPI DADVTVIGSG PGGYVAAIKA
AQLGFKTVCI EKNETLGGTC LNVGCIPSKA LLNNSHYYHM AHGKDFASRG IEMSEVRLNL
DKMMEQKSTA VKALTGGIAH LFKQNKVVHV NGYGKITGKN QVTATKADGG TQVIDTKNIL
IATGSEVTPF PGITIDEDTI VSSTGALSLK KVPEKMVVIG AGVIGVELGS VWQRLGADVT
AVEFLGHVGG VGIDMEISKN FQRILQKQGF KFKLNTKVTG ATKKSDGKID VSIEAASGGK
AEVITCDVLL VCIGRRPFTK NLGLEELGIE LDPRGRIPVN TRFQTKIPNI YAIGDVVAGP
MLAHKAEDEG IICVEGMAGG AVHIDYNCVP SVIYTHPEVA WVGKSEEQLK EEGIEYKVGK
FPFAANSRAK TNADTDGMVK ILGQKSTDRV LGAHILGPGA GEMVNEAALA LEYGASCEDI
ARVCHAHPTL SEAFREANLA ASFGKSINF


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EIAAB11374 Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,LAD,Pig,Sus scrofa
EIAAB11373 Canis familiaris,Canis lupus familiaris,Dihydrolipoamide dehydrogenase,Dihydrolipoyl dehydrogenase, mitochondrial,DLD,Dog
26-849 The enzyme system for cleavage of glycine (glycine cleavage system; EC 2.1.2.10), which is confined to the mitochondria, is composed of 4 protein components P protein (a pyridoxal phosphate-dependent 0.05 mg
GCSH_RAT Rat ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
CSB-EL009335RA Rat Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
E0627h Mouse ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
GCSH_CHICK Chicken ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
TT30A_HUMAN Mouse ELISA Kit FOR Glycine cleavage system H protein, mitochondrial 96T
CSB-EL009335RA Rat Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesRat 96T
CSB-EL009335HU Human Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335BO Bovine Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335CH Chicken Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335MO Mouse Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit 96T
CSB-EL009335HU Human Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesHuman 96T
CSB-EL009335MO Mouse Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesMouse 96T
CSB-EL009335BO Bovine Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesBovine 96T
CSB-EL009335CH Chicken Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesChicken 96T
CSB-EL009335RB Rabbit Glycine cleavage system H protein, mitochondrial(GCSH) ELISA kit SpeciesRabbit 96T
GCSH_MOUSE ELISA Kit FOR Glycine cleavage system H protein, mitochondrial; organism: Mouse; gene name: Gcsh 96T
EIAAB28692 Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex,Lipoyl-containing pyruvate dehydrogenase complex component X,Mouse,Mus musculus,Pdhx,Pyruvate dehydrogenase protein X c


 

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