LGUL_SOYBN
ID LGUL_SOYBN Reviewed; 185 AA.
AC Q9ZS21;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=GmGlyoxI;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=GLXI;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Mandarin;
RX PubMed=10666306; DOI=10.1006/abbi.1999.1596;
RA Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R.;
RT "Cloning and characterization of glyoxalase I from soybean.";
RL Arch. Biochem. Biophys. 374:261-268(2000).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. Active toward
CC the hemithioacetal adducts formed by reacting methylglyoxal or
CC phenylglyoxal with glutathione, homoglutathione or gamma-
CC glutamylcysteine, showing no preference for homoglutathione adducts
CC over glutathione adducts.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal;
CC Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474,
CC ChEBI:CHEBI:57925; EC=4.4.1.5;
CC Evidence={ECO:0000269|PubMed:10666306};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10666306};
CC Note=Binds 3 zinc ions per subunit, but unlike the enzyme from mammals,
CC shows full activity in the absence of metal ions.
CC {ECO:0000269|PubMed:10666306};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24.83 uM for methylglyoxal-glutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC KM=66.02 uM for methylglyoxal-homoglutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC KM=201.78 uM for methylglyoxal-gamma-glutamylcysteine adduct
CC {ECO:0000269|PubMed:10666306};
CC KM=49.32 uM for phenylglyoxal-glutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC KM=26.77 uM for phenylglyoxal-homoglutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC KM=244.83 uM for phenylglyoxal-gamma-glutamylcysteine adduct
CC {ECO:0000269|PubMed:10666306};
CC Vmax=3.00 nmol/sec/mg enzyme toward methylglyoxal-glutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC Vmax=5.70 nmol/sec/mg enzyme toward methylglyoxal-homoglutathione
CC adduct {ECO:0000269|PubMed:10666306};
CC Vmax=7.00 nmol/sec/mg enzyme toward methylglyoxal-gamma-
CC glutamylcysteine adduct {ECO:0000269|PubMed:10666306};
CC Vmax=24.38 nmol/sec/mg enzyme toward phenylglyoxal-glutathione adduct
CC {ECO:0000269|PubMed:10666306};
CC Vmax=21.10 nmol/sec/mg enzyme toward phenylglyoxal-homoglutathione
CC adduct {ECO:0000269|PubMed:10666306};
CC Vmax=83.64 nmol/sec/mg enzyme toward phenylglyoxal-gamma-
CC glutamylcysteine adduct {ECO:0000269|PubMed:10666306};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10666306}.
CC -!- MISCELLANEOUS: Zinc ions may be required for the correct assembly of
CC the enzyme but are not required for catalysis.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR EMBL; AJ010423; CAA09177.1; -; mRNA.
DR RefSeq; NP_001236152.1; NM_001249223.1.
DR RefSeq; XP_006590355.1; XM_006590292.2.
DR AlphaFoldDB; Q9ZS21; -.
DR SMR; Q9ZS21; -.
DR STRING; 3847.GLYMA12G08470.1; -.
DR PRIDE; Q9ZS21; -.
DR GeneID; 547667; -.
DR KEGG; gmx:547667; -.
DR eggNOG; KOG2944; Eukaryota.
DR HOGENOM; CLU_046006_1_3_1; -.
DR InParanoid; Q9ZS21; -.
DR BRENDA; 4.4.1.5; 2483.
DR SABIO-RK; Q9ZS21; -.
DR UniPathway; UPA00619; UER00675.
DR Proteomes; UP000008827; Unplaced.
DR Genevisible; Q9ZS21; GM.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
DR PROSITE; PS51819; VOC; 1.
PE 1: Evidence at protein level;
KW Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..185
FT /note="Lactoylglutathione lyase"
FT /id="PRO_0000391067"
FT DOMAIN 27..174
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 170
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ 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
