A5JTM5 · CBADH_PSEUC

Function

function

Dehalogenates 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA and 4-bromobenzoyl-CoA, but not 4-fluorobenzoyl-CoA. Inactive towards crotonyl-CoA, alpha-methylcrotonyl-CoA and beta-methylcrotonyl-CoA.

Catalytic activity

Activity regulation

Inactivated by 1 mM Ag+ and by 5 mM Cu2+. Partially inhibited by 5 mM Zn2+, Mn2+, Co2+, Fe2+ and Ni2+. Unaffected by 10 mM Na+, K+ and Li+ and by 0.5 mM Mg2+, Mn2+, Fe2+, Ca2+, Co2+ and Zn2+. Inhibited by the sulfhydryl blocking agent 5,5'-dithio-bis-(2-nitrobenzoate), SDS and N-bromosuccinimide. Unaffected by sodium azide and EDTA. Inactivated following treatment with diethyl pyrocarbonate; this inactivation is reversible by treatment with hydroxylamine.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
3.7 μM4-chlorobenzoyl-CoA
4.2 μM4-bromobenzoyl-CoA
6.5 μM4-iodobenzoyl-CoA
10.4 μM2,4-dichlorobenzoyl-CoA
42 μM3,4-dichlorobenzoyl-CoA
30 μM4-chloro-2-nitrobenzoyl-CoA
5.5 μM4-chloro-3-nitrobenzoyl-CoA
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
2.2 μmol/min/mgwith 4-chlorobenzoyl-CoA as substrate

pH Dependence

Optimum pH is 10.0. Half maximum activity remains at pH 9.0 and 11.5. Stable from pH 6.5 to 11.0, activity is lost following 10 minutes incubation at pH 4.5 or 12.0.

Temperature Dependence

Optimum temperature is 60 degrees Celsius. Retains 60% of maximum activity at 30 degrees Celsius and 65 degrees Celsius. After 15 minutes preincubation at 60 degrees Celsius 70% of the initial activity remains, 15 minutes preincubation at 65 degrees Celsius results in a total loss of activity.

Pathway

Xenobiotic degradation; 4-chlorobenzoate degradation; 4-hydroxybenzoate from 4-chlorobenzoate: step 2/3.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site24substrate; ligand shared between two oligomeric partners; in other chain
Binding site62-67substrate; ligand shared between two oligomeric partners; in other chain
Active site90Proton acceptor
Binding site114substrate; ligand shared between two oligomeric partners; in other chain
Active site145Nucleophile
Binding site257substrate; ligand shared between two oligomeric partners

GO annotations

AspectTerm
Molecular Function4-chlorobenzoyl-CoA dehalogenase activity
Biological Processcoenzyme A metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4-chlorobenzoyl coenzyme A dehalogenase
  • EC number
  • Short names
    4-CBA-CoA dehalogenase
    ; 4-CBCoA dehalogenase
    ; 4-chlorobenzoyl-CoA dehalogenase

Organism names

Accessions

  • Primary accession
    A5JTM5

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis24Does not strongly affect catalytic activity, but reduces substrate CoA binding.
Mutagenesis34Forms inclusion bodies.
Mutagenesis43No effect on catalytic activity.
Mutagenesis45No effect on catalytic activity.
Mutagenesis46No effect on catalytic activity.
Mutagenesis63Yields insoluble protein.
Mutagenesis6430-fold reduction in catalytic activity, substrate benzoyl group binding is unaffected.
Mutagenesis64Retains catalytic activity, but substrate benzoyl group binding is decreased.
Mutagenesis64Severely reduces catalytic activity. Arylated intermediate does not accumulate.
Mutagenesis65Catalytic activity is almost as efficient as wild type.
Mutagenesis67Reduces substrate CoA binding.
Mutagenesis67Forms inclusion bodies.
Mutagenesis68No effect on catalytic activity.
Mutagenesis81Loss of catalytic activity, substrate benzoyl group binding is not affected.
Mutagenesis82Retains catalytic activity, but substrate benzoyl group binding is decreased.
Mutagenesis89Retains catalytic activity, but substrate benzoyl group binding is decreased.
Mutagenesis89Reduced activity and substrate benzoyl group binding.
Mutagenesis90Complete loss of catalytic activity (PubMed:8718880, PubMed:9063883).
Significantly reduced activity (PubMed:11695894).
Substrate binding is not significantly affected. Reduced arylated intermediate formation.
Mutagenesis94No effect on catalytic activity.
Mutagenesis112Yields insoluble protein.
Mutagenesis112Protein precipitates upon purification.
Mutagenesis112Catalytic activity is almost as efficient as wild type.
Mutagenesis113Strongly reduced catalytic activity and substrate benzoyl group binding. Arylated intermediate does not accumulate.
Mutagenesis113Strongly reduced catalytic activity. Arylated intermediate does not accumulate.
Mutagenesis113Protein precipitates upon purification.
Mutagenesis114Strongly reduced catalytic activity and substrate benzoyl group binding.
Mutagenesis114Unstable.
Mutagenesis115Yields insoluble protein.
Mutagenesis123No effect on catalytic activity.
Mutagenesis129No effect on catalytic activity.
Mutagenesis137Low catalytic activity, but KM unaffected (PubMed:8718880).
Retains catalytic activity, but substrate benzoyl group binding is decreased (PubMed:9063883).
Mutagenesis145Complete loss of catalytic activity, but not substrate binding.
Mutagenesis163No effect on catalytic activity.
Mutagenesis175No effect on catalytic activity.
Mutagenesis179No effect on catalytic activity.
Mutagenesis208No effect on catalytic activity.
Mutagenesis216Yields insoluble protein.
Mutagenesis232Yields insoluble protein.
Mutagenesis232Reduced catalytic activity, increased substrate binding.
Mutagenesis257Retains catalytic activity and substrate CoA binding.
Mutagenesis257Significantly reduces catalytic activity and substrate CoA binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004011471-2694-chlorobenzoyl coenzyme A dehalogenase

Expression

Induction

By 4-chlorobenzoyl-CoA, 4-iodobenzoyl-CoA or 4-bromobenzoyl-CoA.

Interaction

Subunit

Homotetramer (PubMed:1610806).
Homotetramer, homooctamer and larger multimers (PubMed:7579994).
Homotrimer (PubMed:8679561).

Family & Domains

Sequence similarities

Belongs to the enoyl-CoA hydratase/isomerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    269
  • Mass (Da)
    29,802
  • Last updated
    2007-06-26 v1
  • Checksum
    EC165E9063C70B07
MYEAIGHRVEDGVAEITIKLPRHRNALSVKAMQEVTDALNRAEEDDSVGAVMITGAEDAFCAGFYLREIPLDKGVAGVRDHFRIGALWWHQMIHKIIRVKRPVLAAINGVAAGGGLGISLASDMAICADSAKFVCAWHTIGIGNDTATSYSLARIVGMRRAMELMLTNRTLYPEEAKDWGLVSRVYPKDDFREVAWKVARELAAAPTHLQVMAKERFHAGWMQPVEECTEFEIQNVIASVTHPHFMPCLTEFLDGHRADRPQVELPAGV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF569604
EMBL· GenBank· DDBJ
ABQ44578.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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