EC number:4.4.1.5

Enzyme

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     4. Lyases
        4.4 Carbon-sulfur lyases
            4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
ID:4.4.1.5
Description:Lactoylglutathione lyase.
Alternative Name: Methylglyoxalase.
Ketone-aldehyde mutase.
Glyoxalase I.
Aldoketomutase.
(R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing).
Prosite: PDOC00720;
PDB:
PDBScop
1FA8 8022537; 8034917; 8022537; 8034917;
1FA7 8022537; 8034917; 8022537; 8034917;
1FA6 8022537; 8034917; 8022537; 8034917;
1FA5 8022537; 8034917; 8022537; 8034917;
1F9Z 8022537; 8034917; 8022537; 8034917;
 » show all
Cath: 1.20.1050.10; 3.40.50.880; 3.40.30.10; 3.10.180.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.4.1.5
BRENDA Enzyme Link: BRENDA 4.4.1.5
KEGG Enzyme Link: KEGG4.4.1.5
BioCyc Enzyme Link: BioCyc 4.4.1.5
ExPASy Enzyme Link: ExPASy4.4.1.5
EC2PDB Enzyme Link: EC2PDB 4.4.1.5
ExplorEnz Enzyme Link: ExplorEnz 4.4.1.5
PRIAM enzyme-specific profiles Link: PRIAM 4.4.1.5
IntEnz Enzyme Link: IntEnz 4.4.1.5
MEDLINE Enzyme Link: MEDLINE 4.4.1.5

EC number:4.4.1.5

MSA:

4.4.1.5;
Phylogenetic Tree:

4.4.1.5;
Uniprot:
M-CSA:
RHEA:19069 (R)-S-lactoylglutathione = glutathione + methylglyoxal
RULE(radius=1) [*:1]-[S;H0;+0:2]-[C;H0;+0:3](=[*:4])-[CH;+0:5](-[*:6])-[OH;+0:7]>>[*:1]-[SH;+0:2].[*:4]=[CH;+0:3]-[C;H0;+0:5](-[*:6])=[O;H0;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The stereochemical configuration of the lactoyl group of S-lactoylglutathionine formed by the action of glyoxalase I from porcine erythrocytes and yeast.Ekwall K, Mannervik B1973 Feb 284574550
The mechanism of action of glyoxalase.RACKER E1951 Jun14841219