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Literature summary for 1.13.11.37 extracted from

  • Nordin, K.; Unell, M.; Jansson, J.K.
    Novel 4-chlorophenol degradation gene cluster and degradation route via hydroxyquinol in Arthrobacter chlorophenolicus A6 (2005), Appl. Environ. Microbiol., 71, 6538-6544.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cphA-1 from Arthrobacter chloropenolicus A6 is cloned into the vectro pCRT7/CT-TOPO, the construct is transformed into CL21(DE3)/pLysS cells. Pseudarthrobacter chlorophenolicus A6
cphA-2 from Arthrobacter chloropenolicus A6 is cloned into the vectro pCRT7/CT-TOPO, the construct is transformed into CL21(DE3)/pLysS cells. Pseudarthrobacter chlorophenolicus A6

Protein Variants

Protein Variants Comment Organism
additional information Arthrobacter chlorophenolicus A6 is transformed with plasmid pKGT452Cbeta, which contain an Arthrobacter-derived, randomly inserting transposon conferring chloramphenicol resistance. The transposon mutagenese to disrupt the cphA-1 gene generates mutant strain Arthrobacter chlorophenolicus T99. The T99 mutant is not able to grow on 4-chlorophenol as a sole carbon source and shows a hydroxyquinol accumulation. Pseudarthrobacter chlorophenolicus A6

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
recombinant CphA-1 Pseudarthrobacter chlorophenolicus A6
42000
-
recombinant CphA-2 Pseudarthrobacter chlorophenolicus A6

Organism

Organism UniProt Comment Textmining
Pseudarthrobacter chlorophenolicus A6 Q3BEM2
-
-
Pseudarthrobacter chlorophenolicus A6 Q3BEN0
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
cell extracts from 4-chlorophenol-grown cells deplete hydoxyquinol from the medium with an activity of 96 microM/min/mg protein. No depletion of hydroxyquinol is measured in extracts of Succinate-grown cells. Pseudarthrobacter chlorophenolicus A6
additional information
-
Cph-2 remove hydroxyquinol: CphA-2 = 3.0 microM/min/mg. CphA-2 show some activity with catechol: CphA-2 = 0.15 microM/min/mg. Pseudarthrobacter chlorophenolicus A6
additional information
-
CphA-1 remove hydroxyquinol: CphA-1 = 16 microM/min/mg. CphA-1 show some activity with catechol: CphA-1 = 0.67 microM/min/mg. Pseudarthrobacter chlorophenolicus A6

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information CphA-1 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol Pseudarthrobacter chlorophenolicus A6 ?
-
?
additional information CphA-2 exhibits no activity with 4-chlorocatechol, hydroquinone, or resorcinol Pseudarthrobacter chlorophenolicus A6 ?
-
?

Synonyms

Synonyms Comment Organism
cphA-1
-
Pseudarthrobacter chlorophenolicus A6
cphA-2
-
Pseudarthrobacter chlorophenolicus A6
cphA-I
-
Pseudarthrobacter chlorophenolicus A6
More cphA-1 encode hydroxyquinol 1,2-dioxygenases. The amino acid sequence of CphA-2 is 78.4% identical to that of CphA-1. Pseudarthrobacter chlorophenolicus A6
More cphA-2 encodes hydroxyquinol 1,2-dioxygenases. The amino acid sequence of CphA-2 is 78.4% identical to that of CphA-1. Pseudarthrobacter chlorophenolicus A6