3.7.1.13: 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase

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For detailed information about 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase, go to the full flat file.

Reaction

(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate

Synonyms

CarC, HOPDA hydrolase

ECTree

3 Hydrolases

3.7 Acting on carbon-carbon bonds

3.7.1 In ketonic substances

3.7.1.13 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase

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Results	in table
167	AA Sequence
4	Cloned(Commentary)
1	Cofactor
1	Crystallization (Commentary)
2	kcat/KM [mM/s]
4	KM Value [mM]
9	Molecular Weight [Da]
14	Organism
4	Pathway
2	pH Optimum
3	pH Range
2	Protein Variants
4	Purification (Commentary)
1	Reaction
7	Reference
2	Specific Activity [micromol/min/mg]
19	Substrates and Products (Substrate)
7	Subunits
6	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
2	Temperature Stability [°C]
4	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.7.1.13 - 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase

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Go to Crystallization (commentary) Search

to 1.86 A resolution, space group I422. The subunit of ht-CarCJ3 is divided into two domains, i.e., the core domain with residues 15-144 and 209-282, and the lid domain with residues 145-208. The invisible 10 amino acid residues Ile146-Asn155 correspond to the helix alpha4, which is the putative first alpha-helix in the lid domain. Sidechains of the active-site residues, Ser114 and His261, are clearly shown in the electron density map

Janthinobacterium sp. J3

Q84II3

707350