Escherichia coli K-12 substr. MG1655 Enzyme: glyoxalase II

Gene: gloB Accession Numbers: G6099 (EcoCyc), b0212, ECK0212

Synonyms: yafR

Regulation Summary Diagram: ?

Regulation summary diagram for gloB

Glyoxalase II catalyzes the second of two sequential reactions in the conversion of methylglyoxal to D-lactate [Thornalley90].

The enzyme contains ~1.7 molecules of Zn2+ per active monomer. Co2+ and Mn2+ can substitute for Zn2+, but Ni2+ can not [Oyoung07].

A gloB null mutant accumulates S-lactoylglutathione upon methylglyoxal exposure and has a depleted glutathione pool. This leads to activation of the KefB potassium efflux system, which causes cytoplasmic acidification and protection against methylglyoxal toxicity. Conversely, overexpression of gloB leads to depletion of S-lactoylglutathione and increased sensitivity to methylglyoxal [Ozyamak10].

gloB shows differential codon adaptation, resulting in differential translation efficiency signatures, in thermophilic microbes. It was therefore predicted to play a role in the heat shock response. A gloB deletion mutant was shown to be more sensitive than wild-type specifically to heat shock, but not other stresses [Krisko14]. Single gloB and gloC mutants show decreased methylglyoxal tolerance; a ΔgloBC double deletion mutant is more sensitive to methylglyoxal than either single mutant [Reiger15].

Reviews: [Suttisansanee11, Sukdeo08, Thornalley90]

Locations: cytosol

Map Position: [234,027 <- 234,782] (5.04 centisomes, 18°)
Length: 756 bp / 251 aa

Molecular Weight of Polypeptide: 28.434 kD (from nucleotide sequence), 28.4 kD (experimental) [Oyoung07 ]

Unification Links: ASAP:ABE-0000707 , DIP:DIP-48248N , EchoBASE:EB3114 , EcoGene:EG13330 , EcoliWiki:b0212 , Mint:MINT-1295781 , ModBase:P0AC84 , OU-Microarray:b0212 , PortEco:gloB , Pride:P0AC84 , Protein Model Portal:P0AC84 , RefSeq:NP_414748 , RegulonDB:G6099 , SMR:P0AC84 , String:511145.b0212 , UniProt:P0AC84

Relationship Links: InterPro:IN-FAMILY:IPR001279 , InterPro:IN-FAMILY:IPR017782 , Panther:IN-FAMILY:PTHR11935:SF7 , Pfam:IN-FAMILY:PF00753 , Smart:IN-FAMILY:SM00849

In Paralogous Gene Group: 68 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Krisko14]
GO:0019243 - methylglyoxal catabolic process to D-lactate Inferred from experiment [Oyoung07]
GO:0006750 - glutathione biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004416 - hydroxyacylglutathione hydrolase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Oyoung07]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA01a, Oyoung07]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism methylglyoxal metabolism

Essentiality data for gloB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Last-Curated ? 26-Mar-2015 by Keseler I , SRI International

Enzymatic reaction of: glyoxalase II

Synonyms: hydroxyacylglutathione hydrolase, S-(2-hydroxyacyl)glutathione hydrolase

EC Number:

(R)-S-lactoylglutathione + H2O <=> glutathione + (R)-lactate + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Alternative Products for glutathione [Comment 5 ]: glutathionylspermidine [Mullings12 ]

In Pathways: superpathway of methylglyoxal degradation , methylglyoxal degradation I

Cofactors or Prosthetic Groups: Zn2+ [Oyoung07]

Inhibitors (Unknown Mechanism): Cu2+ [Reiger15]

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)

Sequence Features

Protein sequence of glyoxalase II with features indicated

Feature Class Location Citations Comment
Metal-Binding-Site 53
UniProt: Zinc 1; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 55
UniProt: Zinc 1; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 57
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 58
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 110
UniProt: Zinc 1; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 127
UniProt: Zinc 1; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 165
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Krisko14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

Mullings12: Mullings KY, Sukdeo N, Suttisansanee U, Ran Y, Honek JF (2012). "Ni2+-activated glyoxalase I from Escherichia coli: substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily." J Inorg Biochem 108;133-40. PMID: 22173092

Oyoung07: O'young J, Sukdeo N, Honek JF (2007). "Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme." Arch Biochem Biophys 459(1):20-6. PMID: 17196158

Ozyamak10: Ozyamak E, Black SS, Walker CA, Maclean MJ, Bartlett W, Miller S, Booth IR (2010). "The critical role of S-lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli." Mol Microbiol 78(6);1577-90. PMID: 21143325

Reiger15: Reiger M, Lassak J, Jung K (2015). "Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli." FEMS Microbiol Lett 362(2);1-7. PMID: 25670698

Sukdeo08: Sukdeo N, Honek JF (2008). "Microbial glyoxalase enzymes: metalloenzymes controlling cellular levels of methylglyoxal." Drug Metabol Drug Interact 23(1-2);29-50. PMID: 18533363

Suttisansanee11: Suttisansanee U, Honek JF (2011). "Bacterial glyoxalase enzymes." Semin Cell Dev Biol 22(3);285-92. PMID: 21310258

Thornalley90: Thornalley PJ (1990). "The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life." Biochem J 1990;269(1);1-11. PMID: 2198020

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Tue Oct 6, 2015, biocyc12.