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 |
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 | ? | - |
? |
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 | - |
- |
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 |
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 | ? | - |
? |
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 |
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 |