3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

This is an abbreviated version!
For detailed information about 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, go to the full flat file.

Reaction

Synonyms

2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dieonic acid hydrolase, 6-phenyl HODA hydrolase, BphD, BphD enzyme, BphDP6, CarC, HOHPDA hydrolase, HOPD hydrolase, HOPDA hydrolase, HPDA hydrolase, HsaD, hydrolase, 2,6-dioxo-6-phenylhexa-3-enoate, LigY, MCP hydrolase, meta-cleavage product hydrolase, MhpC

ECTree

     3 Hydrolases

         3.7 Acting on carbon-carbon bonds

             3.7.1 In ketonic substances

                3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

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Results	in table
648	AA Sequence
9	Application
1	CAS Registry Number
16	Cloned(Commentary)
1	Cofactor
8	Crystallization (Commentary)
21	General Information
19	Inhibitors
25	kcat/KM [mM/s]
3	Ki Value [mM]
70	KM Value [mM]
1	Metals/Ions
11	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
83	Organism
7	Pathway
40	PDB ID
6	pH Optimum
3	pH Range
2	pH Stability
53	Protein Variants
15	Purification (Commentary)
8	Reaction
1	Reaction Type
44	Reference
6	Specific Activity [micromol/min/mg]
4	Storage Stability
100	Substrates and Products (Substrate)
14	Subunits
76	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
2	Temperature Range [°C]
4	Temperature Stability [°C]
67	Turnover Number [1/s]

Application

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Application on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

degradation

2 entries

environmental protection

Arthrobacter sp. YC-RL1

A0A0H0ZQK0

potential enzyme resource for the biodegradation of biphenyl, bioremediation of the environmental pollution caused by biphenyl/polychlorinated biphenyls

755881

molecular biology

6 entries

degradation

Rhodococcus globerulus

-

key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders

674232

degradation

Rhodococcus globerulus P6

-

key determinant in the aerobic transformation of polychlorinated biphenyls by divergent biphenyl degraders

-

molecular biology

Pseudomonas sp.

-

open reading frame corresponding to the pcbD gene consists of 855 base pairs with an ATG initiation codon and a TGA termination codon, able to encode a polypeptide with a molecular weight of 31732 containing 284 amino acid residues, deduced amino acid sequence has 62% identity with those of the HOPDA hydrolases of Pseudomonas putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase

675331

molecular biology

Pseudomonas sp.

-

the deduced amino acid sequence of CarC shows 30.3, 31.3, and 31.8% identity with meta-cleavage compound hydrolases TodF, XylF, and DmpD, respectively, from other Pseudomonas

676944

molecular biology

Bacillus sp. (in: Bacteria)

-

upstream of bphC are five ORFs, including bphD, exhibiting low homology with, and a different gene order from, previously characterized bph genes

675835

molecular biology

Pseudomonas sp. LD2

-

the deduced amino acid sequence of CarC shows 30.3, 31.3, and 31.8% identity with meta-cleavage compound hydrolases TodF, XylF, and DmpD, respectively, from other Pseudomonas

-

molecular biology

Pseudomonas sp. P20

-

open reading frame corresponding to the pcbD gene consists of 855 base pairs with an ATG initiation codon and a TGA termination codon, able to encode a polypeptide with a molecular weight of 31732 containing 284 amino acid residues, deduced amino acid sequence has 62% identity with those of the HOPDA hydrolases of Pseudomonas putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase

-

molecular biology

Bacillus sp. (in: Bacteria) JF8

-

upstream of bphC are five ORFs, including bphD, exhibiting low homology with, and a different gene order from, previously characterized bph genes

-