ECMDB

Identification

Name:

Lactoylglutathione lyase

Synonyms:

Aldoketomutase
Glyoxalase I
Glx I
Ketone-aldehyde mutase
Methylglyoxalase
S-D-lactoylglutathione methylglyoxal lyase

Gene Name:

gloA

Enzyme Class:

4.4.1.5

Biological Properties

General Function:

Involved in lactoylglutathione lyase activity

Specific Function:

Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione

Cellular Location:

Not Available

SMPDB Pathways:

Not Available

KEGG Pathways:

Pyruvate metabolism ec00620

KEGG Reactions:

1.0

↔

1.0

1.0Glutathione + 1.0Pyruvaldehyde ↔ 1.0S-Lactoylglutathione
ReactionCard

1.0

↔

1.0

1.0S-Lactoylglutathione ↔ 1.0Glutathione + 1.0Pyruvaldehyde
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.0Pyruvaldehyde + 1.0Glutathione → 1.0S-Lactoylglutathione
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0Glutathione + 1.0Pyruvaldehyde ↔ 1.0S-Lactoylglutathione
ReactionCard

1.0

↔

1.0

1.0S-Lactoylglutathione ↔ 1.0Glutathione + 1.0Pyruvaldehyde
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0S-Lactoylglutathione → 1.0Glutathione + 1.0Pyruvaldehyde
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00125	Glutathione	MetaboCard
ECMDB01167	Pyruvaldehyde	MetaboCard
ECMDB01066	S-Lactoylglutathione	MetaboCard

GO Classification:

Function
binding
carbon-sulfur lyase activity
catalytic activity
cation binding
ion binding
lactoylglutathione lyase activity
lyase activity
metal ion binding

Gene Properties

Blattner:

b1651

Gene Orientation

Clockwise

Centisome Percentage:

37.20

Left Sequence End

1725861

Right Sequence End

1726268

Gene Sequence:

>408 bp
ATGAACATCAGCGATGTAGCAAAAATTACCGGCCTGACCAGCAAAGCCATTCGCTTCTAT
GAAGAGAAGGGGCTGGTGACGCCGCCGATGCGCAGCGAAAACGGTTATCGCACCTACACG
CAGCAGCATCTCAACGAACTGACCTTACTGCGCCAGGCACGGCAGGTGGGCTTTAACCTG
GAAGAGAGCGGCGAGCTGGTGAATCTGTTTAACGACCCGCAGCGGCACAGCGCCGACGTC
AAACGGCGCACGCTGGAGAAGGTGGCGGAGATCGAACGACACATTGAGGAGCTGCAATCC
ATGCGCGACCAGCTGCTGGCACTGGCGAATGCCTGCCCTGGCGATGACAGCGCCGACTGC
CCGATTATCGAAAATCTCTCCGGCTGCTGTCATCATCGGGCAGGGTGA

Protein Properties

Pfam Domain Function:

Glyoxalase (PF00903 )

Protein Residues:

135

Protein Molecular Weight:

14920

Protein Theoretical pI:

PDB File:

1FA8

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Lactoylglutathione lyase
MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYN
WGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYK
IELIEEKDAGRGLGN

References

External Links:

Resource	Link
Uniprot ID:	P0AC81
Uniprot Name:	LGUL_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674626
PDB ID:	1FA8
Ecogene ID:	EG13421
Ecocyc:	EG13421
ColiBase:	b1651
Kegg Gene:	b1651
EchoBASE ID:	EB3197
CCDB:	LGUL_ECOLI
BacMap:	16129609

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Clugston, S. L., Barnard, J. F., Kinach, R., Miedema, D., Ruman, R., Daub, E., Honek, J. F. (1998). "Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: evidence for optimal activation by nickel ions." Biochemistry 37:8754-8763. Pubmed: 9628737
Clugston, S. L., Daub, E., Kinach, R., Miedema, D., Barnard, J. F., Honek, J. F. (1997). "Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences." Gene 186:103-111. Pubmed: 9047352
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
He, M. M., Clugston, S. L., Honek, J. F., Matthews, B. W. (2000). "Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation." Biochemistry 39:8719-8727. Pubmed: 10913283

Lactoylglutathione lyase (P0AC81)