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Literature summary extracted from

  • Chen, S.L.; Fang, W.H.; Himo, F.
    Reaction mechanism of the binuclear zinc enzyme glyoxalase II - A theoretical study (2009), J. Inorg. Biochem., 103, 274-281.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.2.6 Computational study, the bond distances of the bridging hydroxide to the two zinc ions are calculated to be 1.99 and 1.95 A, to be compared to the crystallographic distances of 2.03 and 1.99 A. The computed Zn-Zn distance of 3.29 A is also in very good agreement with the crystallographic distance of 3.34 A. Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.2.6 Zn2+ glyoxalase I is a binuclear zinc-enzyme, Zn2+ stabilizes the charge of tetrahedral intermediate thereby lowering the barrier for the nucleophilic attack, while Zn1 stabilizes the charge of the thiolate product, thereby facilitating the C-S bond cleavage Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.6 additional information Homo sapiens GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved ?
-
 ?
3.1.2.6 additional information Homo sapiens the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins ?
-
 ?
3.1.2.6 additional information Homo sapiens The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction. ?
-
 ?
3.1.2.6 S-D-lactoylglutathione + H2O Homo sapiens
-
 glutathione + D-lactic acid
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.6 Homo sapiens Q16775
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.6 additional information GlxII belongs to the metallo-beta-lactamase superfamily of proteins, in which a zinc-binding motif is conserved Homo sapiens ?
-
 ?
3.1.2.6 additional information the glyoxalase system can detoxify methylglyoxal, a by-product of carbohydrate and lipid metabolism, which can produce toxic effects by reacting with RNA, DNA and proteins Homo sapiens ?
-
 ?
3.1.2.6 additional information The glyoxalase system catalyzes the conversion of toxic methylglyoxal to nontoxic D-lactic acid using glutathione as a coenzyme. Glyoxalase II is a binuclear Zn-enzyme that catalyzes the second step of this conversion, namely the hydrolysis of S-D-lactoylglutathione, which is the product of the glyoxalase I (EC 4.4.15) reaction. Homo sapiens ?
-
 ?
3.1.2.6 S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione + H2O slow model substrate for computational study, the substrate does not coordinate to any of the zinc ions in the Michaelis complex. The hydroxyl group forms a hydrogen bond to the Asp58 residue. Homo sapiens ?
-
 ?
3.1.2.6 S-D-lactoylglutathione + H2O
-
 Homo sapiens glutathione + D-lactic acid
-
 r

Synonyms

EC Number Synonyms Comment Organism
3.1.2.6 GlxII
-
 Homo sapiens
3.1.2.6 glyoxalase II
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.2.6 280
-
 S-D-lactoylglutathione
-
 Homo sapiens