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Literature summary for 3.7.1.14 extracted from

  • Siirola, E.; Frank, A.; Grogan, G.; Kroutil, W.
    C-C hydrolases for biocatalysis (2013), Adv. Synth. Catal., 355, 1677-1691.
No PubMed abstract available
Search for more literature for 3.7.1.14

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme structure determination and analysis, PDB ID 1U2E Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O Escherichia coli the enzyme also catalyses the reverse reaction of C-C hydrolysis, namely C-C bond formation (2Z)-2-hydroxypenta-2,4-dienoate + succinate
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 r
additional information Escherichia coli MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77044
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Reaction

Reaction Comment Organism Reaction ID
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O = (2Z)-2-hydroxypenta-2,4-dienoate + succinate although MCP hydrolases have a catalytic serine in the active site, the mechanism proceeds via a geminal diol, rather than an acyl-enzyme intermediate, reaction mechanism of the hydrolysis reaction, overview. MCP hydrolases accept alternative nucleophiles in addition to water, and accepts hydroxylamine in the C-C cleavage reaction. MhpC has a typical serine-hydrolase catalytic triad (Ser107, Asp228 and His256), but mechanistic studies indicate that the serine in the active site does not act as a nucleophile in the hydrolysis, but rather the reaction proceeds via general base catalysis.The serine in the active site might stabilise the oxyanion intermediate by hydrogen bonding Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate + H2O the enzyme also catalyses the reverse reaction of C-C hydrolysis, namely C-C bond formation Escherichia coli (2Z)-2-hydroxypenta-2,4-dienoate + succinate
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 r
additional information MCP hydrolases catalyse the C-C bond cleavage of compounds with a common structure, 2-hydroxy-6-oxohexa-2,4-dienoate with different substituents at the C-6 carbon Escherichia coli ?
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 ?
additional information the enzyme is able to catalyse carbon-carbon bond formation. In addition to its natural substrate 2-hydroxy-6-oxonona-1,9-dienedioic acid, enzyme MhpC also hydrolyses various analogues and also the hydrolysis of ester bonds of monoethyl adipate and 4-nitrophenyl valerate. The H114A mutant of the enzyme also hydrolyses 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, a substrate of enzyme BphD, EC 3.7.1.8. Incubation of monomethyl succinate and ethyl 2-hydroxypentadienoate with the wild-type freeze-dried MhpC in hexane result in C-C bond formation product Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
2-hydroxy-6-ketonona-1,9-dioic acid 5,6-hydrolase
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 Escherichia coli
MCP hydrolase
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 Escherichia coli
meta-cleavage product hydrolase
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 Escherichia coli
MhpC
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 Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the alpha/beta-hydrolase superfamily Escherichia coli
physiological function the enzyme catalyse the hydrolysis of vinylogous 1,5-diketone meta-cleavage products generated during the biodegradation of various aromatic compounds Escherichia coli