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

 LGUL_SOYBN              Reviewed;         185 AA.
Q9ZS21;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 70.
RecName: Full=Lactoylglutathione lyase;
EC=4.4.1.5;
AltName: Full=Aldoketomutase;
AltName: Full=Glyoxalase I;
Short=GmGlyoxI;
AltName: Full=Ketone-aldehyde mutase;
AltName: Full=Methylglyoxalase;
AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
Name=GLXI;
Glycine max (Soybean) (Glycine hispida).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Glycine; Soja.
NCBI_TaxID=3847;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Mandarin;
PubMed=10666306; DOI=10.1006/abbi.1999.1596;
Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R.;
"Cloning and characterization of glyoxalase I from soybean.";
Arch. Biochem. Biophys. 374:261-268(2000).
-!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
methylglyoxal and glutathione, to S-lactoylglutathione. Active
toward the hemithioacetal adducts formed by reacting methylglyoxal
or phenylglyoxal with glutathione, homoglutathione or gamma-
glutamylcysteine, showing no preference for homoglutathione
adducts over glutathione adducts.
-!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
methylglyoxal. {ECO:0000269|PubMed:10666306}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10666306};
Note=Binds 3 zinc ions per subunit, but unlike the enzyme from
mammals, shows full activity in the absence of metal ions.
{ECO:0000269|PubMed:10666306};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=24.83 uM for methylglyoxal-glutathione adduct
{ECO:0000269|PubMed:10666306};
KM=66.02 uM for methylglyoxal-homoglutathione adduct
{ECO:0000269|PubMed:10666306};
KM=201.78 uM for methylglyoxal-gamma-glutamylcysteine adduct
{ECO:0000269|PubMed:10666306};
KM=49.32 uM for phenylglyoxal-glutathione adduct
{ECO:0000269|PubMed:10666306};
KM=26.77 uM for phenylglyoxal-homoglutathione adduct
{ECO:0000269|PubMed:10666306};
KM=244.83 uM for phenylglyoxal-gamma-glutamylcysteine adduct
{ECO:0000269|PubMed:10666306};
Vmax=3.00 nmol/sec/mg enzyme toward methylglyoxal-glutathione
adduct {ECO:0000269|PubMed:10666306};
Vmax=5.70 nmol/sec/mg enzyme toward methylglyoxal-
homoglutathione adduct {ECO:0000269|PubMed:10666306};
Vmax=7.00 nmol/sec/mg enzyme toward methylglyoxal-gamma-
glutamylcysteine adduct {ECO:0000269|PubMed:10666306};
Vmax=24.38 nmol/sec/mg enzyme toward phenylglyoxal-glutathione
adduct {ECO:0000269|PubMed:10666306};
Vmax=21.10 nmol/sec/mg enzyme toward phenylglyoxal-
homoglutathione adduct {ECO:0000269|PubMed:10666306};
Vmax=83.64 nmol/sec/mg enzyme toward phenylglyoxal-gamma-
glutamylcysteine adduct {ECO:0000269|PubMed:10666306};
-!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
degradation; (R)-lactate from methylglyoxal: step 1/2.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10666306}.
-!- MISCELLANEOUS: Zinc ions may be required for the correct assembly
of the enzyme but are not required for catalysis.
-!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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EMBL; AJ010423; CAA09177.1; -; mRNA.
RefSeq; NP_001236152.1; NM_001249223.1.
RefSeq; XP_006590355.1; XM_006590292.2.
UniGene; Gma.4045; -.
ProteinModelPortal; Q9ZS21; -.
SMR; Q9ZS21; -.
STRING; 3847.GLYMA12G08470.1; -.
GeneID; 547667; -.
KEGG; gmx:547667; -.
eggNOG; ENOG410IU7X; Eukaryota.
eggNOG; ENOG4111FDV; LUCA.
InParanoid; Q9ZS21; -.
KO; K01759; -.
BRENDA; 4.4.1.5; 2483.
SABIO-RK; Q9ZS21; -.
UniPathway; UPA00619; UER00675.
Proteomes; UP000008827; Unplaced.
Genevisible; Q9ZS21; GM.
GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
InterPro; IPR037523; VOC.
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;
Complete proteome; Lyase; Metal-binding; Reference proteome; Zinc.
CHAIN 1 185 Lactoylglutathione lyase.
/FTId=PRO_0000391067.
DOMAIN 27 174 VOC. {ECO:0000255|PROSITE-
ProRule:PRU01163}.
REGION 154 155 Substrate binding. {ECO:0000250}.
ACT_SITE 170 170 Proton donor/acceptor. {ECO:0000250}.
METAL 30 30 Zinc. {ECO:0000250}.
METAL 96 96 Zinc. {ECO:0000250}.
METAL 124 124 Zinc; via tele nitrogen. {ECO:0000250}.
METAL 170 170 Zinc. {ECO:0000250}.
BINDING 30 30 Substrate. {ECO:0000250}.
BINDING 34 34 Substrate. {ECO:0000250}.
BINDING 100 100 Substrate. {ECO:0000250}.
BINDING 120 120 Substrate. {ECO:0000250}.
BINDING 124 124 Substrate. {ECO:0000250}.
SEQUENCE 185 AA; 20960 MW; 1A2C7BD375441915 CRC64;
MAAEPKESPS NNPGLHTTPD EATKGYIMQQ TMFRIKDPKV SLDFYSRVLG MSLLKRLDFP
EMKFSLYFMG YENTAEAPSN PIDKVVWTFS QKATIELTHN WGTESDPEFK GYHNGNSEPR
GFGHIGVTVD DTYKACERFQ NLGVEFVKKP EDGKMKGIAF IKDPDGYWIE IFDRKTIGNV
TQTAA


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