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Literature summary extracted from

  • Honek, J.F.
    Bacterial glyoxalase I enzymes: structural and biochemical investigations (2014), Biochem. Soc. Trans., 42, 479-484.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.4.1.5 additional information the octahedral metal ligand geometry appears to be mechanistically quintessential to Glo1 enzymatic activity, regardless of the Glo1 metal-activation class Clostridium acetobutylicum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.5 the initial high-throughput X-ray structure containing Zn2+ bound in the two active sites shows a trigonal bipyramidal geometry, inactive Zn2+ -bound enzyme, whereas the active Ni2+ -bound enzyme has an octahedral geometry Clostridium acetobutylicum
4.4.1.5 X-ray structure of the homodimeric humanGlo1 in the presence of the bound inhibitor S-benzylglutathione Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.5 S-benzylglutathione
-
Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.5 Cd2+ can partially substitute for Zn2+, the proton-transfer step is partially rate-limiting for the Cd2+ -substituted enzyme utilizing alpha-deuterophenylglyoxal as substrate Escherichia coli
4.4.1.5 Co2+ activates Pseudomonas putida
4.4.1.5 Co2+ can partially substitute for Ni2+ Pseudomonas aeruginosa
4.4.1.5 Mg2+ activates Pseudomonas putida
4.4.1.5 Mn2+ activates Pseudomonas putida
4.4.1.5 additional information broad metal-activation profile of the enzyme, the mechanism probably involves the formation of an enediol(ate) reaction intermediate Pseudomonas putida
4.4.1.5 additional information no activation by Ni2+. The two metals stabilize the transition state, possibly an enediol(ate)-like transition state, to different extents and/or there is a differential contribution to a mechanism that requires exchange of the water ligands on the metal with the oxygens of the substrate hemithioacetal, homodimeric in nature with two subunits identified in the structure,with each active site being formed by residues from each of the two subunits and two water (or hydroxide) molecules completing the octahedral metal-co-ordination environment Escherichia coli
4.4.1.5 additional information no activation by Zn2+ of isozymes 1 and 2 Pseudomonas aeruginosa
4.4.1.5 additional information no activation by Zn2+, trigonal bipyramidal geometry of the inactive Zn2+ -bound enzyme. The octahedral metal ligand geometry appears to be mechanistically quintessential to Glo1 enzymatic activity, regardless of the Glo1 metal-activation class Clostridium acetobutylicum
4.4.1.5 additional information no Zn2+ -activation Leishmania major
4.4.1.5 Ni2+ activates Pseudomonas putida
4.4.1.5 Ni2+ activates isozymes 1 and 2, Ni2+ -activation class Pseudomonas aeruginosa
4.4.1.5 Ni2+ activates, Ni2+ -activation class, only one Ni2+ is needed for full enzyme activation Leishmania major
4.4.1.5 Ni2+ Ni2+-activating class Leishmania donovani
4.4.1.5 Ni2+ Ni2+-activating class Trypanosoma cruzi
4.4.1.5 Ni2+ required for activity, dependent on, Ni2+ -activation class, the active Ni2+ -bound enzyme has an octahedral geometry Clostridium acetobutylicum
4.4.1.5 Zn2+ activates isozyme 3, Zn2+ -activation class Pseudomonas aeruginosa
4.4.1.5 Zn2+ activates, beste metal ion, Zn2+ -activation class Pseudomonas putida
4.4.1.5 Zn2+ activates, Zn2+ -activation class Saccharomyces cerevisiae
4.4.1.5 Zn2+ activates, Zn2+ -activation class Pseudomonas fluorescens
4.4.1.5 Zn2+ activates, Zn2+ -activation class Pseudomonas syringae
4.4.1.5 Zn2+ activates, Zn2+ -activation class. Presence of two active sites, with each active-site Zn2+ ion bound by two amino acid residues from one subunit and two other residues from the second subunit. Water molecules are proximal to the Zn2+ centre. The presence of a repeating betalphabetabetabeta secondary-structural motif is discovered in the molecular structure Homo sapiens
4.4.1.5 Zn2+ Zn2+ -activation class Neisseria meningitidis
4.4.1.5 Zn2+ Zn2+ -activation class Yersinia pestis
4.4.1.5 Zn2+ Zn2+ -activation class, Zn2+ binds to the active site Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.5 glutathione + methylglyoxal Escherichia coli
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Homo sapiens
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Saccharomyces cerevisiae
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Pseudomonas fluorescens
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Pseudomonas aeruginosa
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Pseudomonas putida
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Neisseria meningitidis
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Plasmodium falciparum
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Yersinia pestis
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Pseudomonas syringae
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal Clostridium acetobutylicum
-
(R)-S-lactoylglutathione
-
?
4.4.1.5 trypanothione + methylglyoxal Trypanosoma cruzi
-
S,S'-bis((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal Leishmania donovani
-
5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal Leishmania major
-
5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal Leishmania infantum
-
5,5'-bi((R)-lactoyl)trypanothione
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Clostridium acetobutylicum
-
-
-
4.4.1.5 Escherichia coli
-
-
-
4.4.1.5 Homo sapiens
-
-
-
4.4.1.5 Leishmania donovani
-
-
-
4.4.1.5 Leishmania infantum
-
-
-
4.4.1.5 Leishmania major
-
-
-
4.4.1.5 Neisseria meningitidis
-
-
-
4.4.1.5 Plasmodium falciparum
-
-
-
4.4.1.5 Pseudomonas aeruginosa
-
three isozymes of glyoxalase I
-
4.4.1.5 Pseudomonas fluorescens
-
-
-
4.4.1.5 Pseudomonas putida
-
-
-
4.4.1.5 Pseudomonas syringae
-
-
-
4.4.1.5 Saccharomyces cerevisiae
-
-
-
4.4.1.5 Trypanosoma cruzi
-
-
-
4.4.1.5 Yersinia pestis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.5 glutathione + methylglyoxal
-
Escherichia coli (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Homo sapiens (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Saccharomyces cerevisiae (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Pseudomonas fluorescens (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Pseudomonas aeruginosa (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Pseudomonas putida (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Neisseria meningitidis (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Plasmodium falciparum (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Yersinia pestis (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Pseudomonas syringae (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal
-
Clostridium acetobutylicum (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Escherichia coli (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Homo sapiens (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Saccharomyces cerevisiae (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas fluorescens (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas aeruginosa (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas putida (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Neisseria meningitidis (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Plasmodium falciparum (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Yersinia pestis (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas syringae (R)-S-lactoylglutathione
-
?
4.4.1.5 glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Clostridium acetobutylicum (R)-S-lactoylglutathione
-
?
4.4.1.5 additional information the calculated longer-range electrostatic attractive potential for the enzyme is centred between and above the two active sites, suggesting a possible approach trajectory for the substrate targeted initially to a position above the two active sites followed by migration to one of the two active sites allowing for enzymatic reaction Clostridium acetobutylicum ?
-
?
4.4.1.5 trypanothione + methylglyoxal
-
Trypanosoma cruzi S,S'-bis((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Trypanosoma cruzi S,S'-bis((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal
-
Leishmania donovani 5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal
-
Leishmania major 5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal
-
Leishmania infantum 5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania donovani 5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania major 5,5'-bi((R)-lactoyl)trypanothione
-
?
4.4.1.5 trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania infantum 5,5'-bi((R)-lactoyl)trypanothione
-
?

Subunits

EC Number Subunits Comment Organism
4.4.1.5 dimer
-
Pseudomonas putida
4.4.1.5 dimer quaternary-structure arrangement analysis, overview Clostridium acetobutylicum
4.4.1.5 homodimer
-
Homo sapiens
4.4.1.5 homodimer crystal structure overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.4.1.5 Glo1
-
Escherichia coli
4.4.1.5 Glo1
-
Homo sapiens
4.4.1.5 Glo1
-
Saccharomyces cerevisiae
4.4.1.5 Glo1
-
Pseudomonas fluorescens
4.4.1.5 Glo1
-
Pseudomonas aeruginosa
4.4.1.5 Glo1
-
Pseudomonas putida
4.4.1.5 Glo1
-
Neisseria meningitidis
4.4.1.5 Glo1
-
Leishmania donovani
4.4.1.5 Glo1
-
Trypanosoma cruzi
4.4.1.5 Glo1
-
Plasmodium falciparum
4.4.1.5 Glo1
-
Yersinia pestis
4.4.1.5 Glo1
-
Pseudomonas syringae
4.4.1.5 Glo1
-
Clostridium acetobutylicum
4.4.1.5 Glo1
-
Leishmania major
4.4.1.5 Glo1
-
Leishmania infantum
4.4.1.5 GloA
-
Escherichia coli
4.4.1.5 GloA
-
Homo sapiens
4.4.1.5 GloA
-
Saccharomyces cerevisiae
4.4.1.5 GloA
-
Pseudomonas fluorescens
4.4.1.5 GloA
-
Pseudomonas aeruginosa
4.4.1.5 GloA
-
Pseudomonas putida
4.4.1.5 GloA
-
Neisseria meningitidis
4.4.1.5 GloA
-
Leishmania donovani
4.4.1.5 GloA
-
Trypanosoma cruzi
4.4.1.5 GloA
-
Plasmodium falciparum
4.4.1.5 GloA
-
Yersinia pestis
4.4.1.5 GloA
-
Pseudomonas syringae
4.4.1.5 GloA
-
Clostridium acetobutylicum
4.4.1.5 GloA
-
Leishmania major
4.4.1.5 GloA
-
Leishmania infantum
4.4.1.5 GLXI
-
Escherichia coli
4.4.1.5 GLXI
-
Homo sapiens
4.4.1.5 GLXI
-
Saccharomyces cerevisiae
4.4.1.5 GLXI
-
Pseudomonas fluorescens
4.4.1.5 GLXI
-
Pseudomonas aeruginosa
4.4.1.5 GLXI
-
Pseudomonas putida
4.4.1.5 GLXI
-
Neisseria meningitidis
4.4.1.5 GLXI
-
Leishmania donovani
4.4.1.5 GLXI
-
Trypanosoma cruzi
4.4.1.5 GLXI
-
Plasmodium falciparum
4.4.1.5 GLXI
-
Yersinia pestis
4.4.1.5 GLXI
-
Pseudomonas syringae
4.4.1.5 GLXI
-
Clostridium acetobutylicum
4.4.1.5 GLXI
-
Leishmania major
4.4.1.5 GLXI
-
Leishmania infantum
4.4.1.5 glyoxalase I
-
Escherichia coli
4.4.1.5 glyoxalase I
-
Homo sapiens
4.4.1.5 glyoxalase I
-
Saccharomyces cerevisiae
4.4.1.5 glyoxalase I
-
Pseudomonas fluorescens
4.4.1.5 glyoxalase I
-
Pseudomonas aeruginosa
4.4.1.5 glyoxalase I
-
Pseudomonas putida
4.4.1.5 glyoxalase I
-
Neisseria meningitidis
4.4.1.5 glyoxalase I
-
Leishmania donovani
4.4.1.5 glyoxalase I
-
Trypanosoma cruzi
4.4.1.5 glyoxalase I
-
Plasmodium falciparum
4.4.1.5 glyoxalase I
-
Yersinia pestis
4.4.1.5 glyoxalase I
-
Pseudomonas syringae
4.4.1.5 glyoxalase I
-
Clostridium acetobutylicum
4.4.1.5 glyoxalase I
-
Leishmania major
4.4.1.5 glyoxalase I
-
Leishmania infantum
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Escherichia coli
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Homo sapiens
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Saccharomyces cerevisiae
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Pseudomonas fluorescens
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Pseudomonas aeruginosa
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Pseudomonas putida
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Neisseria meningitidis
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Leishmania donovani
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Trypanosoma cruzi
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Plasmodium falciparum
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Yersinia pestis
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Pseudomonas syringae
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Clostridium acetobutylicum
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Leishmania major
4.4.1.5 S-D-lactoylglutathione methylglyoxal lyase (isomerizing)
-
Leishmania infantum