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InterPro: IPR004361 Glyoxalase I

Protein matches Help

UniProtKB

Matches:

800 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004361 Glyoxalase_1

Secondary

IPR000325

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR00068	glyox_I	800
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004360 Glyoxalase/bleomycin resistance protein/dioxygenase

Contains

IPR018146 Glyoxalase I, conserved site

GO Term annotation Help

Function

GO:0004462 lactoylglutathione lyase activity
GO:0046872 metal ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction:

glutathione + methylglyoxal = (R)-S-lactoylglutathione

S-lactoylglutathione is then converted by glyoxalase II to lactic acid [1]. Glyoxalase I is a ubiquitous enzyme which binds one mole of zinc per subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. In bacteria and mammals the enzyme is a protein of about 130 to 180 residues while in fungi it is about twice as long. In these organisms the enzyme is built out of the tandem repeat of a homologous domain.

Structural links Help

PDB - click here

SCOP: d.32.1.1

CATH: 3.10.180.10

Database links Help

PDBe-motif: PS00934 , PS00935

Enzyme: EC:4.4.1.5

PROSITE doc: PDOC00720

Blocks: IPB004361

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004361

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P50107 Lactoylglutathione lyase

Q04760 Lactoylglutathione lyase

Q8H0V3 Lactoylglutathione lyase

Q948T6 Lactoylglutathione lyase

Q9CPU0 Lactoylglutathione lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004361	Glyoxalase I
IPR004360	Glyoxalase/bleomycin resistance protein/dioxygenase
IPR018146	Glyoxalase I, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Kim NS, 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 11217-21 1993 [PubMed: 7684374] http://intl.jbc.org/cgi/reprint/268/15/11217.pdf

Additional Reading Open in usermanual
	Ariza A, Vickers TJ, Greig N, Armour KA, Dixon MJ, Eggleston IM, Fairlamb AH, Bond CS. Specificity of the trypanothione-dependent Leishmania major glyoxalase I: structure and biochemical comparison with the human enzyme. Mol. Microbiol. 59 2006 1239-48 [PubMed: 16430697] http://dx.doi.org/10.1111/j.1365-2958.2006.05022.x
	He MM, Clugston SL, Honek JF, Matthews BW. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry 39 2000 8719-27 [PubMed: 10913283] http://dx.doi.org/10.1021/bi000856g
	Ridderstrom M, Cameron AD, Jones TA, Mannervik B. Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I. J. Biol. Chem. 273 1998 21623-8 [PubMed: 9705294] http://dx.doi.org/10.1074/jbc.273.34.21623
	Cameron AD, Ridderstrom M, Olin B, Kavarana MJ, Creighton DJ, 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 1999 13480-90 [PubMed: 10521255] http://dx.doi.org/10.1021/bi990696c
	Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA. Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping. EMBO J. 16 1997 3386-95 [PubMed: 9218781] http://dx.doi.org/10.1093/emboj/16.12.3386

InterPro 23.1