Enzymes
| UniProtKB help_outline | 44 proteins |
| Enzyme class help_outline |
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- Name help_outline 2,6-dioxo-6-phenylhexa-3-enoate Identifier CHEBI:64675 Charge -1 Formula C12H9O4 InChIKeyhelp_outline QPGAZPBFRAAJBD-UHFFFAOYSA-M SMILEShelp_outline [H]C(CC(=O)c1ccccc1)=CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-oxopent-4-enoate Identifier CHEBI:11641 Charge -1 Formula C5H5O3 InChIKeyhelp_outline NOXRYJAWRSNUJD-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)C(=O)CC=C 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline benzoate Identifier CHEBI:16150 (CAS: 766-76-7) help_outline Charge -1 Formula C7H5O2 InChIKeyhelp_outline WPYMKLBDIGXBTP-UHFFFAOYSA-M SMILEShelp_outline [O-]C(=O)c1ccccc1 2D coordinates Mol file for the small molecule Search links Involved in 17 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:17161 | RHEA:17162 | RHEA:17163 | RHEA:17164 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Selection of Pseudomonas sp. strain HBP1 Prp for metabolism of 2-propylphenol and elucidation of the degradative pathway.
Kohler H.P., van der Maarel M.J., Kohler-Staub D.
A mutant of Pseudomonas sp. strain HBP1, originally isolated on 2-hydroxybiphenyl, was selected for the ability to grow on 2-propylphenol as the sole carbon and energy source. In the mutant strain, which was designated as Pseudomonas sp. strain HBP1 Prp, the cellular induction mechanism involved i ... >> More
A mutant of Pseudomonas sp. strain HBP1, originally isolated on 2-hydroxybiphenyl, was selected for the ability to grow on 2-propylphenol as the sole carbon and energy source. In the mutant strain, which was designated as Pseudomonas sp. strain HBP1 Prp, the cellular induction mechanism involved in the synthesis of the NADH-dependent monooxygenase is changed. 2-Propylphenol, which is known to be a substrate of the monooxygenase, does not induce formation of the monooxygenase in the wild type but does have an induction effect in the mutant strain. Furthermore, in contrast to the wild type, mutant strain HBP1 Prp constitutively produces a small amount of monooxygenase and metapyrocatechase. The enzymes from strain HBP1 Prp catalyzing the first three steps in the degradation of 2-propylphenol--the NADH-dependent monooxygenase, the metapyrocatechase, and the meta fission product hydrolase--were partially purified, and their activities were measured. The product of the monooxygenase activity was identified by mass spectrometry as 3-propylcatechol. The metapyrocatechase used this compound as a substrate and produced a yellow meta fission product that was identified by mass spectrometry as 2-hydroxy-6-oxo-nona-2,4-dienoate. Butyrate could be detected as a product of the meta fission product hydrolase in crude cell extract of 2-propylphenol-grown cells, as well as an intermediate in culture broths during growth on 2-propylphenol. All three enzymes expressed highest activities for the metabolites of the degradation of 2-hydroxybiphenyl. << Less
Appl Environ Microbiol 59:860-866(1993) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
Comments
Published in Omori, T., Sugimura, K., Ishigooka, H. and Minoda, Y. Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl. Agric. Biol. Chem. 50 (1986) 931-937.