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Literature summary for 3.7.1.8 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 3.7.1.8

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme structure determination and analysis, PDB ID 1C4X Rhodococcus sp.
enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ Paraburkholderia xenovorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,6-dioxo-6-phenylhexa-3-enoate + H2O Paraburkholderia xenovorans
-
 benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O Rhodococcus sp.
-
 benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O Rhodococcus sp. RHA1
-
 benzoate + 2-oxopent-4-enoate
-
 ?
additional information Paraburkholderia xenovorans 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 ?
-
 ?
additional information Rhodococcus sp. 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 ?
-
 ?
additional information Rhodococcus sp. RHA1 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Paraburkholderia xenovorans P47229 i.e. Pseudomonas LB400
-
Rhodococcus sp. Q75WN8
-
-
Rhodococcus sp. RHA1 Q75WN8
-
-

Reaction

Reaction Comment Organism Reaction ID
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate 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. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview Paraburkholderia xenovorans
a
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate 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. The Ser-His-Asp triad containing enzyme BphD most likely shows the formation of a covalent acyl enzyme intermediate, reaction mechanism, overview Rhodococcus sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,6-dioxo-6-phenylhexa-3-enoate + H2O
-
 Paraburkholderia xenovorans benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
-
 Rhodococcus sp. benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues Paraburkholderia xenovorans benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues Rhodococcus sp. benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O
-
 Rhodococcus sp. RHA1 benzoate + 2-oxopent-4-enoate
-
 ?
2,6-dioxo-6-phenylhexa-3-enoate + H2O enzyme BphD catalyses the hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, HOPDA, and many substrate analogues Rhodococcus sp. RHA1 benzoate + 2-oxopent-4-enoate
-
 ?
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 Paraburkholderia xenovorans ?
-
 ?
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 Rhodococcus sp. ?
-
 ?
additional information enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates Paraburkholderia xenovorans ?
-
 ?
additional information enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates Rhodococcus sp. ?
-
 ?
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 Rhodococcus sp. RHA1 ?
-
 ?
additional information enzyme BphD accepts small alcohols such as methanol, ethanol, n-propanol and 2-propanol as nucleophiles in C-C bond cleavage of 2,6-dioxo-6-phenylhexa-3-enoate, thereby directly forming benzoate esters.Iin addition to the hydrolysis of C-C bonds, BphD also hydrolyses the ester bond in para-substituted nitrophenyl benzoates Rhodococcus sp. RHA1 ?
-
 ?

Synonyms

Synonyms Comment Organism
BphD
-
 Paraburkholderia xenovorans
BphD
-
 Rhodococcus sp.
MCP hydrolase
-
 Paraburkholderia xenovorans
MCP hydrolase
-
 Rhodococcus sp.
meta-cleavage product hydrolase
-
 Paraburkholderia xenovorans
meta-cleavage product hydrolase
-
 Rhodococcus sp.

General Information

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