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Literature summary for 4.4.1.5 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

Activating Compound Comment Organism Structure
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)

Crystallization (Comment) Organism
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
X-ray structure of the homodimeric humanGlo1 in the presence of the bound inhibitor S-benzylglutathione Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
S-benzylglutathione
-
Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
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
Co2+ activates Pseudomonas putida
Co2+ can partially substitute for Ni2+ Pseudomonas aeruginosa
Mg2+ activates Pseudomonas putida
Mn2+ activates Pseudomonas putida
additional information broad metal-activation profile of the enzyme, the mechanism probably involves the formation of an enediol(ate) reaction intermediate Pseudomonas putida
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
additional information no activation by Zn2+ of isozymes 1 and 2 Pseudomonas aeruginosa
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
additional information no Zn2+ -activation Leishmania major
Ni2+ activates Pseudomonas putida
Ni2+ activates isozymes 1 and 2, Ni2+ -activation class Pseudomonas aeruginosa
Ni2+ activates, Ni2+ -activation class, only one Ni2+ is needed for full enzyme activation Leishmania major
Ni2+ Ni2+-activating class Leishmania donovani
Ni2+ Ni2+-activating class Trypanosoma cruzi
Ni2+ required for activity, dependent on, Ni2+ -activation class, the active Ni2+ -bound enzyme has an octahedral geometry Clostridium acetobutylicum
Zn2+ activates isozyme 3, Zn2+ -activation class Pseudomonas aeruginosa
Zn2+ activates, beste metal ion, Zn2+ -activation class Pseudomonas putida
Zn2+ activates, Zn2+ -activation class Saccharomyces cerevisiae
Zn2+ activates, Zn2+ -activation class Pseudomonas fluorescens
Zn2+ activates, Zn2+ -activation class Pseudomonas syringae
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
Zn2+ Zn2+ -activation class Neisseria meningitidis
Zn2+ Zn2+ -activation class Yersinia pestis
Zn2+ Zn2+ -activation class, Zn2+ binds to the active site Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + methylglyoxal
-
Escherichia coli (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Homo sapiens (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Saccharomyces cerevisiae (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Pseudomonas fluorescens (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Pseudomonas aeruginosa (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Pseudomonas putida (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Neisseria meningitidis (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Plasmodium falciparum (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Yersinia pestis (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Pseudomonas syringae (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal
-
Clostridium acetobutylicum (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Escherichia coli (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Homo sapiens (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Saccharomyces cerevisiae (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas fluorescens (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas aeruginosa (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas putida (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Neisseria meningitidis (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Plasmodium falciparum (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Yersinia pestis (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Pseudomonas syringae (R)-S-lactoylglutathione
-
?
glutathione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Clostridium acetobutylicum (R)-S-lactoylglutathione
-
?
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 ?
-
?
trypanothione + methylglyoxal
-
Trypanosoma cruzi S,S'-bis((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Trypanosoma cruzi S,S'-bis((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal
-
Leishmania donovani 5,5'-bi((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal
-
Leishmania major 5,5'-bi((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal
-
Leishmania infantum 5,5'-bi((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania donovani 5,5'-bi((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania major 5,5'-bi((R)-lactoyl)trypanothione
-
?
trypanothione + methylglyoxal the reverse reaction from the hemithioacetate intermediate proceeds non-enzymatically Leishmania infantum 5,5'-bi((R)-lactoyl)trypanothione
-
?

Subunits

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

Synonyms

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