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Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase)

 LGUL_HUMAN              Reviewed;         184 AA.
Q04760; B2R6P7; B4DDV0; P78375; Q59EL0; Q5TZW3; Q96FC0; Q96J41;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 4.
25-OCT-2017, entry version 184.
RecName: Full=Lactoylglutathione lyase;
EC=4.4.1.5;
AltName: Full=Aldoketomutase;
AltName: Full=Glyoxalase I;
Short=Glx I;
AltName: Full=Ketone-aldehyde mutase;
AltName: Full=Methylglyoxalase;
AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
Name=GLO1;
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 ALA-111.
PubMed=7684374;
Kim N.-S., Umezawa Y., Ohmura S., Kato S.;
"Human glyoxalase I. cDNA cloning, expression, and sequence similarity
to glyoxalase I from Pseudomonas putida.";
J. Biol. Chem. 268:11217-11221(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-111.
TISSUE=Colon;
PubMed=8449929;
Ranganathan S., Walsh E.S., Godwin A.K., Tew K.D.;
"Cloning and characterization of human colon glyoxalase-I.";
J. Biol. Chem. 268:5661-5667(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8670058;
Ridderstroem M., Mannervik B.;
"Optimized heterologous expression of the human zinc enzyme glyoxalase
I.";
Biochem. J. 314:463-467(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-111.
PubMed=10564821; DOI=10.1016/S0378-1119(99)00420-5;
Ranganathan S., Ciaccio P.J., Walsh E.S., Tew K.D.;
"Genomic sequence of human glyoxalase-I: analysis of promoter activity
and its regulation.";
Gene 240:149-155(1999).
[5]
NUCLEOTIDE SEQUENCE [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 MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS TYR-19 AND ALA-111.
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
TYR-19 AND ALA-111.
TISSUE=Brain, Eye, and Uterus;
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]
PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT
CYS-139, AND DISULFIDE BONDS.
TISSUE=Erythrocyte;
PubMed=20454679; DOI=10.1371/journal.pone.0010399;
Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K.,
Birkemeyer C.;
"Posttranslational modification of human glyoxalase 1 indicates redox-
dependent regulation.";
PLoS ONE 5:E10399-E10399(2010).
[11]
IDENTIFICATION OF NITRIC OXIDE-MODIFIED FORM, PHOSPHORYLATION, AND
MUTAGENESIS OF CYS-19; CYS-20; CYS-61 AND CYS-139.
PubMed=17576200; DOI=10.1042/BJ20070379;
de Hemptinne V., Rondas D., Vandekerckhove J., Vancompernolle K.;
"Tumour necrosis factor induces phosphorylation primarily of the
nitric-oxide-responsive form of glyoxalase I.";
Biochem. J. 407:121-128(2007).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
FUNCTION, PHOSPHORYLATION AT THR-107, AND MUTAGENESIS OF CYS-19;
CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
PubMed=19199007; DOI=10.1007/s11010-009-0031-7;
de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.;
"Phosphorylation on Thr-106 and NO-modification of glyoxalase I
suppress the TNF-induced transcriptional activity of NF-kappaB.";
Mol. Cell. Biochem. 325:169-178(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, 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).
[15]
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).
[16]
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[18]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
S-BENZYL-GLUTATHIONE AND ZINC.
PubMed=9218781; DOI=10.1093/emboj/16.12.3386;
Cameron A.D., Olin B., Ridderstroem M., Mannervik B., Jones T.A.;
"Crystal structure of human glyoxalase I -- evidence for gene
duplication and 3D domain swapping.";
EMBO J. 16:3386-3395(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC AND
S-HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, ACTIVE
SITE, SUBUNIT, AND MUTAGENESIS OF GLN-34; GLU-100 AND GLU-173.
PubMed=9705294; DOI=10.1074/jbc.273.34.21623;
Ridderstroem M., Cameron A.D., Jones T.A., Mannervik B.;
"Involvement of an active-site Zn2+ ligand in the catalytic mechanism
of human glyoxalase I.";
J. Biol. Chem. 273:21623-21628(1998).
[20]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEXES WITH
S-(N-HYDROXY-N-IODOPHENYLCARBAMOYL)GLUTATHIONE;
S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE AND ZINC, AND ACTIVE SITE.
PubMed=10521255; DOI=10.1021/bi990696c;
Cameron A.D., Ridderstroem M., Olin B., Kavarana M.J., Creighton D.J.,
Mannervik B.;
"Reaction mechanism of glyoxalase I explored by an X-ray
crystallographic analysis of the human enzyme in complex with a
transition state analogue.";
Biochemistry 38:13480-13490(1999).
[21]
X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH SYNTHETIC
INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
COFACTOR.
PubMed=23122816; DOI=10.1016/j.bmcl.2012.10.045;
Chiba T., Ohwada J., Sakamoto H., Kobayashi T., Fukami T.A., Irie M.,
Miura T., Ohara K., Koyano H.;
"Design and evaluation of azaindole-substituted N-hydroxypyridones as
glyoxalase I inhibitors.";
Bioorg. Med. Chem. Lett. 22:7486-7489(2012).
-!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
methylglyoxal and glutathione, to S-lactoylglutathione. Involved
in the regulation of TNF-induced transcriptional activity of NF-
kappa-B. Required for normal osteoclastogenesis.
{ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9705294}.
-!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
methylglyoxal. {ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9705294}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9705294};
Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions
are bound between subunits. {ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9705294};
-!- ENZYME REGULATION: Regulated by oxidation of Cys-139 in response
to the redox state of the cell. Results in the alternative
formation of cystine or glutathione-bound cysteine, the latter
modification leading to reduced enzyme activity.
{ECO:0000269|PubMed:20454679}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.3 mM for methylglyoxal/glutathione (native form)
{ECO:0000269|PubMed:20454679};
KM=0.7 mM for methylglyoxal/glutathione (reduced form)
{ECO:0000269|PubMed:20454679};
Vmax=0.335 umol/min/mg enzyme with methylglyoxal/glutathione as
substrate (native form) {ECO:0000269|PubMed:20454679};
Vmax=0.7 umol/min/mg enzyme with methylglyoxal/glutathione as
substrate (reduced form) {ECO:0000269|PubMed:20454679};
Note=Reduction of GLO1 was carried out by incubation with 20 mM
betamercaptoethanol prior to kinetic analysis.;
-!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
degradation; (R)-lactate from methylglyoxal: step 1/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q04760-1; Sequence=Displayed;
Name=2;
IsoId=Q04760-2; Sequence=VSP_041632;
Note=No experimental confirmation available.;
-!- PTM: Glutathionylation at Cys-139 inhibits enzyme activity.
{ECO:0000269|PubMed:20454679}.
-!- PTM: Phosphorylated at Thr-107 in the presence of CaMK2. However,
this is a consensus site for phosphorylation by CK2 so
phosphorylation may be mediated by CK2 rather than CaMK2.
Phosphorylation is induced by TNF and suppresses the TNF-induced
transcriptional activity of NF-kappa-B.
{ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007}.
-!- PTM: Exists in a nitric oxide (NO)-modified form. The exact nature
of the modification is unknown, but it suppresses the TNF-induced
transcriptional activity of NF-kappa-B.
-!- MASS SPECTROMETRY: Mass=20687.4; Method=Electrospray; Range=2-184
(Q04760-1); Note=Variant Glu-111.;
Evidence={ECO:0000269|PubMed:20454679};
-!- MASS SPECTROMETRY: Mass=20629.7; Method=Electrospray; Range=2-184
(Q04760-1); Note=Variant Ala-111.;
Evidence={ECO:0000269|PubMed:20454679};
-!- POLYMORPHISM: Exists in three separable isoforms which originate
from two alleles in the genome. These correspond to two homodimers
and one heterodimer composed of two subunits showing different
electrophoretic properties.
-!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93038.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; D13315; BAA02572.1; -; mRNA.
EMBL; L07837; AAA52565.1; -; mRNA.
EMBL; S83285; AAB49495.1; -; mRNA.
EMBL; AF146651; AAD38008.1; -; Genomic_DNA.
EMBL; AB209801; BAD93038.1; ALT_INIT; mRNA.
EMBL; AK293345; BAG56861.1; -; mRNA.
EMBL; AK312662; BAG35544.1; -; mRNA.
EMBL; BT019987; AAV38790.1; -; mRNA.
EMBL; BT019988; AAV38791.1; -; mRNA.
EMBL; AL391415; CAI21586.1; -; Genomic_DNA.
EMBL; BC001741; AAH01741.1; -; mRNA.
EMBL; BC011365; AAH11365.1; -; mRNA.
EMBL; BC015934; AAH15934.1; -; mRNA.
CCDS; CCDS4837.1; -. [Q04760-1]
PIR; A46714; A46714.
PIR; S63603; S63603.
RefSeq; NP_006699.2; NM_006708.2. [Q04760-1]
UniGene; Hs.268849; -.
PDB; 1BH5; X-ray; 2.20 A; A/B/C/D=2-184.
PDB; 1FRO; X-ray; 2.20 A; A/B/C/D=2-184.
PDB; 1QIN; X-ray; 2.00 A; A/B=2-184.
PDB; 1QIP; X-ray; 1.72 A; A/B/C/D=2-184.
PDB; 3VW9; X-ray; 1.47 A; A/B=1-184.
PDB; 3W0T; X-ray; 1.35 A; A/B/C/D=1-184.
PDB; 3W0U; X-ray; 1.70 A; A/B=1-184.
PDBsum; 1BH5; -.
PDBsum; 1FRO; -.
PDBsum; 1QIN; -.
PDBsum; 1QIP; -.
PDBsum; 3VW9; -.
PDBsum; 3W0T; -.
PDBsum; 3W0U; -.
ProteinModelPortal; Q04760; -.
SMR; Q04760; -.
BioGrid; 109001; 43.
IntAct; Q04760; 4.
STRING; 9606.ENSP00000362463; -.
BindingDB; Q04760; -.
ChEMBL; CHEMBL2424; -.
DrugBank; DB03345; Beta-Mercaptoethanol.
DrugBank; DB00143; Glutathione.
DrugBank; DB00328; Indomethacin.
DrugBank; DB03330; S-(N-Hydroxy-N-Iodophenylcarbamoyl)Glutathione.
DrugBank; DB03602; S-Benzyl-Glutathione.
DrugBank; DB04132; S-Hexylglutathione.
DrugBank; DB03130; S-P-Nitrobenzyloxycarbonylglutathione.
iPTMnet; Q04760; -.
PhosphoSitePlus; Q04760; -.
SwissPalm; Q04760; -.
BioMuta; GLO1; -.
DMDM; 134039205; -.
OGP; Q04760; -.
REPRODUCTION-2DPAGE; IPI00220766; -.
REPRODUCTION-2DPAGE; Q04760; -.
EPD; Q04760; -.
PaxDb; Q04760; -.
PeptideAtlas; Q04760; -.
PRIDE; Q04760; -.
DNASU; 2739; -.
Ensembl; ENST00000373365; ENSP00000362463; ENSG00000124767. [Q04760-1]
GeneID; 2739; -.
KEGG; hsa:2739; -.
CTD; 2739; -.
DisGeNET; 2739; -.
EuPathDB; HostDB:ENSG00000124767.6; -.
GeneCards; GLO1; -.
HGNC; HGNC:4323; GLO1.
HPA; CAB040541; -.
HPA; CAB040542; -.
HPA; HPA059791; -.
MIM; 138750; gene.
neXtProt; NX_Q04760; -.
OpenTargets; ENSG00000124767; -.
PharmGKB; PA28724; -.
eggNOG; ENOG410IU7X; Eukaryota.
eggNOG; ENOG4111FDV; LUCA.
GeneTree; ENSGT00390000009312; -.
HOVERGEN; HBG025852; -.
InParanoid; Q04760; -.
KO; K01759; -.
OMA; NWGTESY; -.
OrthoDB; EOG091G0GMY; -.
PhylomeDB; Q04760; -.
TreeFam; TF105011; -.
BRENDA; 4.4.1.5; 2681.
Reactome; R-HSA-70268; Pyruvate metabolism.
SABIO-RK; Q04760; -.
UniPathway; UPA00619; UER00675.
ChiTaRS; GLO1; human.
EvolutionaryTrace; Q04760; -.
GeneWiki; GLO1; -.
GeneWiki; Lactoylglutathione_lyase; -.
GenomeRNAi; 2739; -.
PRO; PR:Q04760; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124767; -.
CleanEx; HS_GLO1; -.
ExpressionAtlas; Q04760; baseline and differential.
Genevisible; Q04760; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
GO; GO:0009438; P:methylglyoxal metabolic process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
Gene3D; 3.10.180.10; -; 1.
InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
InterPro; IPR004361; Glyoxalase_1.
InterPro; IPR018146; Glyoxalase_1_CS.
Pfam; PF00903; Glyoxalase; 1.
SUPFAM; SSF54593; SSF54593; 1.
TIGRFAMs; TIGR00068; glyox_I; 1.
PROSITE; PS00934; GLYOXALASE_I_1; 1.
PROSITE; PS00935; GLYOXALASE_I_2; 1.
PROSITE; PS51819; VOC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glutathionylation; Lyase;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:20454679}.
CHAIN 2 184 Lactoylglutathione lyase.
/FTId=PRO_0000168076.
DOMAIN 31 177 VOC. {ECO:0000255|PROSITE-
ProRule:PRU01163}.
REGION 157 158 Substrate binding.
ACT_SITE 173 173 Proton donor/acceptor.
{ECO:0000269|PubMed:10521255,
ECO:0000269|PubMed:9705294}.
METAL 34 34 Zinc; shared with dimeric partner.
{ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9218781,
ECO:0000269|PubMed:9705294}.
METAL 100 100 Zinc; shared with dimeric partner.
{ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9218781,
ECO:0000269|PubMed:9705294}.
METAL 127 127 Zinc; via tele nitrogen.
{ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9218781,
ECO:0000269|PubMed:9705294}.
METAL 173 173 Zinc. {ECO:0000269|PubMed:23122816,
ECO:0000269|PubMed:9218781,
ECO:0000269|PubMed:9705294}.
BINDING 34 34 Substrate; shared with dimeric partner.
BINDING 38 38 Substrate; shared with dimeric partner.
BINDING 104 104 Substrate; shared with dimeric partner.
BINDING 123 123 Substrate.
BINDING 127 127 Substrate.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:20454679}.
MOD_RES 88 88 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9CPU0}.
MOD_RES 107 107 Phosphothreonine.
{ECO:0000269|PubMed:19199007}.
MOD_RES 139 139 S-glutathionyl cysteine; alternate.
{ECO:0000269|PubMed:20454679}.
MOD_RES 148 148 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 148 148 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9CPU0}.
DISULFID 19 20 {ECO:0000269|PubMed:20454679}.
DISULFID 61 139 Alternate. {ECO:0000269|PubMed:20454679}.
VAR_SEQ 105 119 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041632.
VARIANT 19 19 C -> Y (in dbSNP:rs17855424).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_031078.
VARIANT 111 111 E -> A (in dbSNP:rs4746).
{ECO:0000269|PubMed:10564821,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7684374,
ECO:0000269|PubMed:8449929}.
/FTId=VAR_013481.
MUTAGEN 19 19 C->A: No effect on NO-mediated
modification. Impaired NO-mediated
modification; when associated with A-20.
Loss of NO-mediated modification; when
associated with A-139.
{ECO:0000269|PubMed:17576200,
ECO:0000269|PubMed:19199007}.
MUTAGEN 20 20 C->A: No effect on NO-mediated
modification. Impaired NO-mediated
modification; when associated with A-19.
Loss of NO-mediated modification; when
associated with A-139.
{ECO:0000269|PubMed:17576200,
ECO:0000269|PubMed:19199007}.
MUTAGEN 34 34 Q->E: Reduces enzyme activity by 99%.
{ECO:0000269|PubMed:9705294}.
MUTAGEN 45 45 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 61 61 C->A: No effect on NO-mediated
modification.
{ECO:0000269|PubMed:17576200}.
MUTAGEN 69 69 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 94 94 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 98 98 T->A: No effect on phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 100 100 E->Q: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:9705294}.
MUTAGEN 102 102 T->A: No effect on phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 107 107 T->A: Loss of phosphorylation.
{ECO:0000269|PubMed:19199007}.
MUTAGEN 139 139 C->A: Impaired NO-mediated modification.
Loss of NO-mediated modification; when
associated with A-19 or A-20.
{ECO:0000269|PubMed:17576200,
ECO:0000269|PubMed:19199007}.
MUTAGEN 173 173 E->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:9705294}.
HELIX 13 18 {ECO:0000244|PDB:3W0T}.
HELIX 25 27 {ECO:0000244|PDB:3W0T}.
STRAND 31 38 {ECO:0000244|PDB:3W0T}.
HELIX 42 51 {ECO:0000244|PDB:3W0T}.
STRAND 56 63 {ECO:0000244|PDB:3W0T}.
TURN 64 67 {ECO:0000244|PDB:3W0T}.
STRAND 68 75 {ECO:0000244|PDB:3W0T}.
HELIX 78 80 {ECO:0000244|PDB:3W0T}.
HELIX 85 92 {ECO:0000244|PDB:3W0T}.
STRAND 95 104 {ECO:0000244|PDB:3W0T}.
HELIX 107 109 {ECO:0000244|PDB:3W0T}.
STRAND 118 122 {ECO:0000244|PDB:3W0T}.
STRAND 124 131 {ECO:0000244|PDB:3W0T}.
HELIX 135 144 {ECO:0000244|PDB:3W0T}.
STRAND 149 151 {ECO:0000244|PDB:3W0T}.
STRAND 155 158 {ECO:0000244|PDB:3W0T}.
STRAND 162 165 {ECO:0000244|PDB:3W0T}.
STRAND 171 175 {ECO:0000244|PDB:3W0T}.
HELIX 177 179 {ECO:0000244|PDB:3W0T}.
HELIX 181 183 {ECO:0000244|PDB:3W0T}.
SEQUENCE 184 AA; 20778 MW; 46291B7878070028 CRC64;
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK
CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS
DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM
ATLM


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