Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7)

 ACADM_HUMAN             Reviewed;         421 AA.
P11310; Q5T4U4; Q9NYF1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
05-JUL-2017, entry version 201.
RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial;
Short=MCAD;
EC=1.3.8.7;
Flags: Precursor;
Name=ACADM;
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).
PubMed=3035565; DOI=10.1073/pnas.84.12.4068;
Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W.,
Strauss A.W.;
"Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and
its expression in enzyme-deficient human tissue.";
Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=1731887; DOI=10.1021/bi00116a013;
Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L.,
Whelan A.J., Strauss A.W.;
"Structural organization and regulatory regions of the human medium-
chain acyl-CoA dehydrogenase gene.";
Biochemistry 31:81-89(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Colon;
Sun F., Wang Y., Block G.D.;
"Medium-chain acyl-CoA dehydrogenase.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart;
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 GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
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).
[8]
PROTEIN SEQUENCE OF 218-235, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, AND VARIANT ACADMD
GLU-329.
PubMed=2393404; DOI=10.1016/0006-291X(90)91421-N;
Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M.,
Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R.;
"Identification of a common mutation in patients with medium-chain
acyl-CoA dehydrogenase deficiency.";
Biochem. Biophys. Res. Commun. 171:498-505(1990).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-301, 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).
[11]
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).
[12]
DEACETYLATION BY SIRT3.
PubMed=24121500; DOI=10.1074/jbc.M113.510354;
Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M.,
Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E.,
Gibson B.W., Hirschey M.D., Goetzman E.S.;
"SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating
conserved lysines near the active site.";
J. Biol. Chem. 288:33837-33847(2013).
[13]
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).
[14]
FUNCTION.
PubMed=25416781; DOI=10.1074/jbc.M114.614115;
Malecki J., Ho A.Y., Moen A., Dahl H.A., Falnes P.O.;
"Human METTL20 is a mitochondrial lysine methyltransferase that
targets the beta subunit of electron transfer flavoprotein (ETFbeta)
and modulates its activity.";
J. Biol. Chem. 290:423-434(2015).
[15]
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).
[16]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND THE
SUBSTRATE ANALOG OCTANOYL-COENZYME A, COFACTOR, AND SUBUNIT.
PubMed=8823176; DOI=10.1021/bi9607867;
Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P.;
"Crystal structures of the wild type and the Glu376Gly/Thr255Glu
mutant of human medium-chain acyl-CoA dehydrogenase: influence of the
location of the catalytic base on substrate specificity.";
Biochemistry 35:12412-12420(1996).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD
AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100;
ILE-108; GLU-237 AND GLU-384, AND SUBUNIT.
PubMed=15159392; DOI=10.1074/jbc.M404884200;
Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S.,
Leys D.;
"Extensive domain motion and electron transfer in the human electron
transferring flavoprotein.medium chain acyl-CoA dehydrogenase
complex.";
J. Biol. Chem. 279:32904-32912(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE
ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384,
AND SUBUNIT.
PubMed=15975918; DOI=10.1074/jbc.M505562200;
Toogood H.S., van Thiel A., Scrutton N.S., Leys D.;
"Stabilization of non-productive conformations underpins rapid
electron transfer to electron-transferring flavoprotein.";
J. Biol. Chem. 280:30361-30366(2005).
[19]
REVIEW ON VARIANTS ACADMD.
PubMed=1363805; DOI=10.1002/humu.1380010402;
Tanaka K., Yokota I., Coates P.M., Strauss A.W., Kelly D.P.,
Zhang Z.F., Gregersen N., Andresen B.S., Matsubara Y., Curtis D.,
Chen Y.-T.;
"Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene.";
Hum. Mutat. 1:271-279(1992).
[20]
VARIANT ACADMD GLU-329.
PubMed=2394825; DOI=10.1172/JCI114761;
Yokota I., Indo Y., Coates P.M., Tanaka K.;
"Molecular basis of medium chain acyl-coenzyme A dehydrogenase
deficiency. An A to G transition at position 985 that causes a lysine-
304 to glutamate substitution in the mature protein is the single
prevalent mutation.";
J. Clin. Invest. 86:1000-1003(1990).
[21]
VARIANT ACADMD GLU-329.
PubMed=2251268; DOI=10.1073/pnas.87.23.9236;
Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G.,
Gregersen N., Dorland L., Strauss A.W.;
"Molecular characterization of inherited medium-chain acyl-CoA
dehydrogenase deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990).
[22]
VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375.
PubMed=1684086;
Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K.;
"Molecular survey of a prevalent mutation, 985A-to-G transition, and
identification of five infrequent mutations in the medium-chain Acyl-
CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency.";
Am. J. Hum. Genet. 49:1280-1291(1991).
[23]
VARIANT ACADMD GLU-329.
PubMed=1902818; DOI=10.1007/BF00201539;
Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N.,
Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S.,
Bolund L., Ghisla S.;
"Molecular characterization of medium-chain acyl-CoA dehydrogenase
(MCAD) deficiency: identification of a lys329 to glu mutation in the
MCAD gene, and expression of inactive mutant enzyme protein in E.
coli.";
Hum. Genet. 86:545-551(1991).
[24]
VARIANT ACADMD GLU-329 FREQUENCY.
PubMed=1671131; DOI=10.1016/0140-6736(91)90907-7;
Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S.,
Gregersen N., Curtis D.;
"Frequency of the G985 MCAD mutation in the general population.";
Lancet 337:298-299(1991).
[25]
VARIANTS ACADMD THR-326 AND ARG-336.
PubMed=8198141;
Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V.,
Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K.,
Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N.;
"Disease-causing mutations in exon 11 of the medium-chain acyl-CoA
dehydrogenase gene.";
Am. J. Hum. Genet. 54:975-988(1994).
[26]
VARIANT ACADMD 115-GLY-CYS-116 DEL.
PubMed=7603790; DOI=10.1203/00006450-199505000-00021;
Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C.,
Strauss A.W., Naylor E.W.;
"Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania:
neonatal screening shows high incidence and unexpected mutation
frequencies.";
Pediatr. Res. 37:675-678(1995).
[27]
VARIANT ACADMD ARG-195.
PubMed=7929823; DOI=10.1172/JCI117486;
Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M.,
Demartinville B., Rinaldo P., Slaugh R., Strauss A.W.;
"A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden
neonatal death.";
J. Clin. Invest. 94:1477-1483(1994).
[28]
VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352.
PubMed=9158144; DOI=10.1093/hmg/6.5.695;
Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S.,
Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K.,
Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L.,
Koelvraa S., Gregersen N.;
"The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD)
deficiency in compound heterozygous patients: is there correlation
between genotype and phenotype?";
Hum. Mol. Genet. 6:695-707(1997).
[29]
CHARACTERIZATION OF VARIANT ACADMD ALA-193.
PubMed=9882619; DOI=10.1042/bj3370225;
Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I.,
Ghisla S.;
"Biochemical characterization of a variant human medium-chain acyl-CoA
dehydrogenase with a disease-associated mutation localized in the
active site.";
Biochem. J. 337:225-230(1999).
[30]
VARIANTS ACADMD LEU-206 AND GLU-329.
PubMed=10767181; DOI=10.1006/mgme.2000.2978;
Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L.,
Dasouki M.J., Wilkinson J., Roe C.R.;
"Identification of a novel mutation in patients with medium-chain
acyl-CoA dehydrogenase deficiency.";
Mol. Genet. Metab. 69:259-262(2000).
[31]
VARIANTS ACADMD HIS-67; THR-78; ILE-121 AND ARG-310.
PubMed=11349232; DOI=10.1086/320602;
Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J.,
McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I.,
Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N.;
"Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by
MS/MS-based prospective screening of newborns differ from those
observed in patients with clinical symptoms: identification and
characterization of a new, prevalent mutation that results in mild
MCAD deficiency.";
Am. J. Hum. Genet. 68:1408-1418(2001).
[32]
VARIANT ACADMD LEU-245.
PubMed=11409868; DOI=10.1007/s004390100501;
Zschocke J., Schulze A., Lindner M., Fiesel S., Olgemoller K.,
Hoffmann G.F., Penzien J., Ruiter J.P.N., Wanders R.J.A.,
Mayatepek E.;
"Molecular and functional characterization of mild MCAD deficiency.";
Hum. Genet. 108:404-408(2001).
[33]
VARIANTS ACADMD THR-281 AND GLU-329.
PubMed=11486912; DOI=10.1023/A:1010533408635;
Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D.;
"Compound heterozygosity in four asymptomatic siblings with medium-
chain acyl-CoA dehydrogenase deficiency.";
J. Inherit. Metab. Dis. 24:417-418(2001).
[34]
VARIANT [LARGE SCALE ANALYSIS] ARG-132.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Acyl-CoA dehydrogenase specific for acyl chain lengths
of 4 to 16 that catalyzes the initial step of fatty acid beta-
oxidation. Utilizes the electron transfer flavoprotein (ETF) as an
electron acceptor to transfer electrons to the main mitochondrial
respiratory chain via ETF-ubiquinone oxidoreductase (ETF
dehydrogenase). {ECO:0000269|PubMed:25416781}.
-!- CATALYTIC ACTIVITY: A medium-chain acyl-CoA + electron-transfer
flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced
electron-transfer flavoprotein.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:8823176};
-!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
oxidation.
-!- SUBUNIT: Homotetramer. Interacts with the heterodimeric electron
transfer flavoprotein ETF. {ECO:0000269|PubMed:15159392,
ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11310-1; Sequence=Displayed;
Name=2;
IsoId=P11310-2; Sequence=VSP_038420;
-!- PTM: Acetylation at Lys-307 and Lys-311 in proximity of the
cofactor-binding sites reduces catalytic activity (By similarity).
These sites are deacetylated by SIRT3. {ECO:0000250}.
-!- DISEASE: Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD)
[MIM:201450]: An inborn error of mitochondrial fatty acid beta-
oxidation which causes fasting hypoglycemia, hepatic dysfunction
and encephalopathy, often resulting in death in infancy.
{ECO:0000269|PubMed:10767181, ECO:0000269|PubMed:11349232,
ECO:0000269|PubMed:11409868, ECO:0000269|PubMed:11486912,
ECO:0000269|PubMed:1363805, ECO:0000269|PubMed:1671131,
ECO:0000269|PubMed:1684086, ECO:0000269|PubMed:1902818,
ECO:0000269|PubMed:2251268, ECO:0000269|PubMed:2393404,
ECO:0000269|PubMed:2394825, ECO:0000269|PubMed:7603790,
ECO:0000269|PubMed:7929823, ECO:0000269|PubMed:8198141,
ECO:0000269|PubMed:9158144, ECO:0000269|PubMed:9882619}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
of different substrate specificities are present in mammalian
tissues.
-!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M16827; AAA51566.1; -; mRNA.
EMBL; M91432; AAA59567.1; -; Genomic_DNA.
EMBL; M91421; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91422; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91423; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91425; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91426; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91427; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91428; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91429; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91430; AAA59567.1; JOINED; Genomic_DNA.
EMBL; M91431; AAA59567.1; JOINED; Genomic_DNA.
EMBL; AF251043; AAF63626.1; -; mRNA.
EMBL; AK312629; BAG35514.1; -; mRNA.
EMBL; AL357314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06401.1; -; Genomic_DNA.
EMBL; BC005377; AAH05377.1; -; mRNA.
EMBL; M60505; AAB59625.1; -; Genomic_DNA.
CCDS; CCDS44165.1; -. [P11310-2]
CCDS; CCDS668.1; -. [P11310-1]
PIR; A29031; DEHUCM.
RefSeq; NP_000007.1; NM_000016.5. [P11310-1]
RefSeq; NP_001120800.1; NM_001127328.2. [P11310-2]
UniGene; Hs.445040; -.
PDB; 1EGC; X-ray; 2.60 A; A/B/C/D=26-421.
PDB; 1EGD; X-ray; 2.40 A; A/B/C/D=26-421.
PDB; 1EGE; X-ray; 2.75 A; A/B/C/D=26-421.
PDB; 1T9G; X-ray; 2.90 A; A/B/C/D=26-421.
PDB; 2A1T; X-ray; 2.80 A; A/B/C/D=1-421.
PDB; 4P13; X-ray; 1.73 A; A/B/C/D=35-421.
PDBsum; 1EGC; -.
PDBsum; 1EGD; -.
PDBsum; 1EGE; -.
PDBsum; 1T9G; -.
PDBsum; 2A1T; -.
PDBsum; 4P13; -.
ProteinModelPortal; P11310; -.
SMR; P11310; -.
BioGrid; 106552; 50.
DIP; DIP-34281N; -.
IntAct; P11310; 9.
MINT; MINT-3007693; -.
STRING; 9606.ENSP00000409612; -.
DrugBank; DB03415; 3-Thiaoctanoyl-Coenzyme A.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB02910; Octanoyl-Coenzyme A.
SwissLipids; SLP:000001334; -.
iPTMnet; P11310; -.
PhosphoSitePlus; P11310; -.
SwissPalm; P11310; -.
BioMuta; ACADM; -.
DMDM; 113017; -.
REPRODUCTION-2DPAGE; IPI00005040; -.
UCD-2DPAGE; P11310; -.
EPD; P11310; -.
MaxQB; P11310; -.
PaxDb; P11310; -.
PeptideAtlas; P11310; -.
PRIDE; P11310; -.
DNASU; 34; -.
Ensembl; ENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
Ensembl; ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneID; 34; -.
KEGG; hsa:34; -.
UCSC; uc001dgw.6; human. [P11310-1]
CTD; 34; -.
DisGeNET; 34; -.
GeneCards; ACADM; -.
GeneReviews; ACADM; -.
HGNC; HGNC:89; ACADM.
HPA; HPA006198; -.
HPA; HPA026542; -.
MalaCards; ACADM; -.
MIM; 201450; phenotype.
MIM; 607008; gene.
neXtProt; NX_P11310; -.
OpenTargets; ENSG00000117054; -.
Orphanet; 42; Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKB; PA24425; -.
eggNOG; KOG0140; Eukaryota.
eggNOG; COG1960; LUCA.
GeneTree; ENSGT00760000119007; -.
HOGENOM; HOG000131659; -.
HOVERGEN; HBG000224; -.
InParanoid; P11310; -.
KO; K00249; -.
PhylomeDB; P11310; -.
TreeFam; TF105020; -.
BioCyc; MetaCyc:HS04089-MONOMER; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
Reactome; R-HSA-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
Reactome; R-HSA-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RK; P11310; -.
UniPathway; UPA00660; -.
EvolutionaryTrace; P11310; -.
GenomeRNAi; 34; -.
PRO; PR:P11310; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117054; -.
CleanEx; HS_ACADM; -.
ExpressionAtlas; P11310; baseline and differential.
Genevisible; P11310; HS.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:BHF-UCL.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IDA:BHF-UCL.
GO; GO:0045329; P:carnitine biosynthetic process; IMP:BHF-UCL.
GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:UniProtKB.
GO; GO:0051793; P:medium-chain fatty acid catabolic process; IDA:BHF-UCL.
GO; GO:0051791; P:medium-chain fatty acid metabolic process; IDA:BHF-UCL.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
CDD; cd01157; MCAD; 1.
Gene3D; 1.10.540.10; -; 1.
InterPro; IPR006089; Acyl-CoA_DH_CS.
InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
InterPro; IPR009075; AcylCo_DH/oxidase_C.
InterPro; IPR013786; AcylCoA_DH/ox_N.
InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
InterPro; IPR034180; MCAD.
Pfam; PF00441; Acyl-CoA_dh_1; 1.
Pfam; PF02770; Acyl-CoA_dh_M; 1.
Pfam; PF02771; Acyl-CoA_dh_N; 1.
SUPFAM; SSF47203; SSF47203; 1.
SUPFAM; SSF56645; SSF56645; 1.
PROSITE; PS00072; ACYL_COA_DH_1; 1.
PROSITE; PS00073; ACYL_COA_DH_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; FAD;
Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 25 Mitochondrion.
CHAIN 26 421 Medium-chain specific acyl-CoA
dehydrogenase, mitochondrial.
/FTId=PRO_0000000502.
NP_BIND 158 167 FAD. {ECO:0000269|PubMed:8823176}.
NP_BIND 191 193 FAD. {ECO:0000269|PubMed:8823176}.
NP_BIND 306 308 FAD. {ECO:0000269|PubMed:8823176}.
NP_BIND 316 317 FAD. {ECO:0000269|PubMed:8823176}.
NP_BIND 374 378 FAD. {ECO:0000269|PubMed:8823176}.
NP_BIND 403 405 FAD. {ECO:0000269|PubMed:8823176}.
REGION 278 281 Substrate binding.
ACT_SITE 401 401 Proton acceptor.
BINDING 167 167 Substrate; via carbonyl oxygen.
BINDING 216 216 Substrate.
BINDING 402 402 Substrate; via amide nitrogen.
BINDING 413 413 Substrate.
MOD_RES 69 69 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 69 69 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 179 179 N6-succinyllysine.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 212 212 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 212 212 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 217 217 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 217 217 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 259 259 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 259 259 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 271 271 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 271 271 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P45952}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 301 301 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 351 351 Phosphothreonine.
{ECO:0000250|UniProtKB:P45952}.
VAR_SEQ 10 10 R -> RCSLQ (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_038420.
VARIANT 53 53 R -> C (in ACADMD; dbSNP:rs398123072).
/FTId=VAR_000317.
VARIANT 67 67 Y -> H (in ACADMD; mild;
dbSNP:rs121434280).
{ECO:0000269|PubMed:11349232}.
/FTId=VAR_013698.
VARIANT 78 78 I -> T (in ACADMD; dbSNP:rs398123074).
{ECO:0000269|PubMed:11349232}.
/FTId=VAR_015954.
VARIANT 115 116 Missing (in ACADMD).
{ECO:0000269|PubMed:7603790}.
/FTId=VAR_000318.
VARIANT 116 116 C -> Y (in ACADMD; dbSNP:rs875989859).
{ECO:0000269|PubMed:9158144}.
/FTId=VAR_015955.
VARIANT 121 121 T -> I (in ACADMD; dbSNP:rs121434283).
{ECO:0000269|PubMed:11349232}.
/FTId=VAR_015956.
VARIANT 132 132 P -> R (in a breast cancer sample;
somatic mutation; dbSNP:rs875989854).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035716.
VARIANT 149 149 M -> I (in ACADMD; dbSNP:rs121434277).
{ECO:0000269|PubMed:1684086}.
/FTId=VAR_000319.
VARIANT 193 193 T -> A (in ACADMD; the thermostability is
markedly decreased; dbSNP:rs121434279).
{ECO:0000269|PubMed:9158144,
ECO:0000269|PubMed:9882619}.
/FTId=VAR_000320.
VARIANT 195 195 G -> R (in ACADMD; dbSNP:rs121434278).
{ECO:0000269|PubMed:7929823}.
/FTId=VAR_000321.
VARIANT 206 206 R -> L (in ACADMD).
{ECO:0000269|PubMed:10767181}.
/FTId=VAR_015957.
VARIANT 244 244 C -> R (in ACADMD; dbSNP:rs121434276).
{ECO:0000269|PubMed:1684086}.
/FTId=VAR_000322.
VARIANT 245 245 S -> L (in ACADMD; dbSNP:rs121434281).
{ECO:0000269|PubMed:11409868}.
/FTId=VAR_013699.
VARIANT 267 267 G -> R (in ACADMD; dbSNP:rs121434274).
{ECO:0000269|PubMed:1684086}.
/FTId=VAR_000323.
VARIANT 281 281 R -> T (in ACADMD; mild or benign
clinical phenotype; dbSNP:rs121434282).
{ECO:0000269|PubMed:11486912}.
/FTId=VAR_013700.
VARIANT 310 310 G -> R (in ACADMD; dbSNP:rs747268471).
{ECO:0000269|PubMed:11349232}.
/FTId=VAR_015958.
VARIANT 326 326 M -> T (in ACADMD; dbSNP:rs786204631).
{ECO:0000269|PubMed:8198141}.
/FTId=VAR_000324.
VARIANT 329 329 K -> E (in ACADMD; most common variant;
dbSNP:rs77931234).
{ECO:0000269|PubMed:10767181,
ECO:0000269|PubMed:11486912,
ECO:0000269|PubMed:1902818,
ECO:0000269|PubMed:2251268,
ECO:0000269|PubMed:2393404,
ECO:0000269|PubMed:2394825}.
/FTId=VAR_000325.
VARIANT 336 336 S -> R (in ACADMD).
{ECO:0000269|PubMed:8198141}.
/FTId=VAR_000326.
VARIANT 352 352 Y -> C (in ACADMD).
{ECO:0000269|PubMed:9158144}.
/FTId=VAR_015959.
VARIANT 375 375 I -> T (in ACADMD; dbSNP:rs121434275).
{ECO:0000269|PubMed:1684086}.
/FTId=VAR_000327.
MUTAGEN 86 86 L->M: Strongly reduced rate of electron
transfer to ETF.
{ECO:0000269|PubMed:15159392}.
MUTAGEN 98 98 L->W: Strongly reduced rate of electron
transfer to ETF.
{ECO:0000269|PubMed:15159392}.
MUTAGEN 100 100 L->Y: Strongly reduced rate of electron
transfer to ETF.
{ECO:0000269|PubMed:15159392}.
MUTAGEN 108 108 I->M: Strongly reduced rate of electron
transfer to ETF.
{ECO:0000269|PubMed:15159392}.
MUTAGEN 191 191 W->A: Loss of electron transfer to ETF.
{ECO:0000269|PubMed:15975918}.
MUTAGEN 191 191 W->F: Reduces rate of electron transfer
to ETF about six-fold.
{ECO:0000269|PubMed:15975918}.
MUTAGEN 237 237 E->A: Strongly reduced rate of electron
transfer to ETF.
{ECO:0000269|PubMed:15159392,
ECO:0000269|PubMed:15975918}.
MUTAGEN 384 384 E->A: Reduces rate of electron transfer
to ETF three-fold.
{ECO:0000269|PubMed:15159392,
ECO:0000269|PubMed:15975918}.
MUTAGEN 384 384 E->Q: Reduces rate of electron transfer
to ETF two-fold.
{ECO:0000269|PubMed:15159392,
ECO:0000269|PubMed:15975918}.
CONFLICT 356 356 I -> T (in Ref. 3; AAF63626).
{ECO:0000305}.
STRAND 36 38 {ECO:0000244|PDB:1EGD}.
HELIX 43 58 {ECO:0000244|PDB:4P13}.
HELIX 61 70 {ECO:0000244|PDB:4P13}.
HELIX 75 83 {ECO:0000244|PDB:4P13}.
HELIX 93 95 {ECO:0000244|PDB:4P13}.
HELIX 102 115 {ECO:0000244|PDB:4P13}.
HELIX 117 136 {ECO:0000244|PDB:4P13}.
HELIX 139 145 {ECO:0000244|PDB:4P13}.
HELIX 147 151 {ECO:0000244|PDB:4P13}.
STRAND 155 159 {ECO:0000244|PDB:4P13}.
STRAND 165 167 {ECO:0000244|PDB:4P13}.
HELIX 169 171 {ECO:0000244|PDB:4P13}.
STRAND 175 179 {ECO:0000244|PDB:4P13}.
STRAND 182 193 {ECO:0000244|PDB:4P13}.
TURN 194 197 {ECO:0000244|PDB:4P13}.
STRAND 198 206 {ECO:0000244|PDB:4P13}.
HELIX 215 218 {ECO:0000244|PDB:4P13}.
STRAND 219 225 {ECO:0000244|PDB:4P13}.
STRAND 231 236 {ECO:0000244|PDB:4P13}.
STRAND 239 241 {ECO:0000244|PDB:4P13}.
STRAND 247 258 {ECO:0000244|PDB:4P13}.
HELIX 259 261 {ECO:0000244|PDB:4P13}.
STRAND 262 265 {ECO:0000244|PDB:4P13}.
TURN 266 268 {ECO:0000244|PDB:1EGE}.
HELIX 269 303 {ECO:0000244|PDB:4P13}.
STRAND 309 312 {ECO:0000244|PDB:1EGC}.
HELIX 313 315 {ECO:0000244|PDB:4P13}.
HELIX 317 345 {ECO:0000244|PDB:4P13}.
HELIX 351 376 {ECO:0000244|PDB:4P13}.
HELIX 377 381 {ECO:0000244|PDB:4P13}.
HELIX 387 394 {ECO:0000244|PDB:4P13}.
HELIX 395 398 {ECO:0000244|PDB:4P13}.
STRAND 400 402 {ECO:0000244|PDB:4P13}.
HELIX 404 417 {ECO:0000244|PDB:4P13}.
SEQUENCE 421 AA; 46588 MW; 7CD0B5832410581B CRC64;
MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI
IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ
TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM
GQRCSDTRGI VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF
AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK
N


Related products :

Catalog number Product name Quantity
18-003-42286 Medium-chain specific acyl-CoA dehydrogenase. mitochondrial - EC 1.3.99.3; MCAD Polyclonal 0.1 mg Protein A
CF46 Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial ACADM 500
CF46 Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial ACADM lmg
ER422 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial Elisa Kit 96T
CD02 Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial ACADM 50
C150 Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial ACADM l0
CSB-EL001126RA Rat Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit 96T
CSB-EL001126BO Bovine Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit 96T
CSB-EL001126HU Human Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit 96T
CSB-EL001126MO Mouse Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit 96T
CSB-EL001126RA Rat Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit SpeciesRat 96T
CSB-EL001126PI Pig Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit SpeciesPig 96T
CSB-EL001126BO Bovine Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit SpeciesBovine 96T
CSB-EL001126MO Mouse Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit SpeciesMouse 96T
CSB-EL001126HU Human Medium-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADM) ELISA kit SpeciesHuman 96T
E10433m ELISA Kit FOR Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; organism: Mouse; gene name: Acadm 96T
ARP32789_T200 Anti-Acyl-CoA dehydrogenase, medium-chain specific, mitochondrial precursor(ACADM) Species_Reactivity: Human
25-092 ACADM Is the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. 0.05 mg
27-708 ACADM Is the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. 0.1 mg
CF46 Recombinant Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial_ACADM 1 mg
CF46 Recombinant Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial_ACADM 50 ug
CF46 Recombinant Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial_ACADM 10 ug
CF46 Recombinant Human Medium-Chain Specific Acyl-CoA Dehydrogenase Mitochondrial_ACADM 500 ug
ACADL_PIG Pig ELISA Kit FOR Long-chain specific acyl-CoA dehydrogenase, mitochondrial 96T
CSB-EL001129RA Rat Very long-chain specific acyl-CoA dehydrogenase, mitochondrial(ACADVL) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur