Any feedback?
Literature summary extracted from
- C-C hydrolases for biocatalysis (2013), Adv. Synth. Catal., 355, 1677-1691.
No PubMed abstract available
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.7.1.8 | enzyme structure determination and analysis, PDB ID 1C4X | Rhodococcus sp. |
| 3.7.1.8 | enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ | Paraburkholderia xenovorans |
| 3.7.1.14 | enzyme structure determination and analysis, PDB ID 1U2E | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | Paraburkholderia xenovorans | - |
benzoate + 2-oxopent-4-enoate | - |
? |  |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | Rhodococcus sp. | - |
benzoate + 2-oxopent-4-enoate | - |
? | |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | Rhodococcus sp. RHA1 | - |
benzoate + 2-oxopent-4-enoate | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.14 | (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 | - |
r | |
| 3.7.1.14 | 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 | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.7.1.8 | Paraburkholderia xenovorans | P47229 | i.e. Pseudomonas LB400 | - |
| 3.7.1.8 | Rhodococcus sp. | Q75WN8 | - |
- |
| 3.7.1.8 | Rhodococcus sp. RHA1 | Q75WN8 | - |
- |
| 3.7.1.14 | Escherichia coli | P77044 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.7.1.8 | 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 | |
| 3.7.1.8 | 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. | |
| 3.7.1.14 | (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 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | - |
Paraburkholderia xenovorans | benzoate + 2-oxopent-4-enoate | - |
? | |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | - |
Rhodococcus sp. | benzoate + 2-oxopent-4-enoate | - |
? | |
| 3.7.1.8 | 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 | - |
? | |
| 3.7.1.8 | 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 | - |
? | |
| 3.7.1.8 | 2,6-dioxo-6-phenylhexa-3-enoate + H2O | - |
Rhodococcus sp. RHA1 | benzoate + 2-oxopent-4-enoate | - |
? | |
| 3.7.1.8 | 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 | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.8 | 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. | ? | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.8 | 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. | ? | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.8 | 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 | ? | - |
? | |
| 3.7.1.14 | (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 | - |
r | |
| 3.7.1.14 | 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 | ? | - |
? | |
| 3.7.1.14 | 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 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.7.1.8 | BphD | - |
Paraburkholderia xenovorans |
| 3.7.1.8 | BphD | - |
Rhodococcus sp. |
| 3.7.1.8 | MCP hydrolase | - |
Paraburkholderia xenovorans |
| 3.7.1.8 | MCP hydrolase | - |
Rhodococcus sp. |
| 3.7.1.8 | meta-cleavage product hydrolase | - |
Paraburkholderia xenovorans |
| 3.7.1.8 | meta-cleavage product hydrolase | - |
Rhodococcus sp. |
| 3.7.1.14 | 2-hydroxy-6-ketonona-1,9-dioic acid 5,6-hydrolase | - |
Escherichia coli |
| 3.7.1.14 | MCP hydrolase | - |
Escherichia coli |
| 3.7.1.14 | meta-cleavage product hydrolase | - |
Escherichia coli |
| 3.7.1.14 | MhpC | - |
Escherichia coli |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.7.1.8 | evolution | the enzyme belongs to the alpha/beta-hydrolase superfamily | Paraburkholderia xenovorans |
| 3.7.1.8 | evolution | the enzyme belongs to the alpha/beta-hydrolase superfamily | Rhodococcus sp. |
| 3.7.1.8 | 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 |
| 3.7.1.8 | 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. |
| 3.7.1.14 | evolution | the enzyme belongs to the alpha/beta-hydrolase superfamily | Escherichia coli |
| 3.7.1.14 | 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
