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Literature summary for 1.14.13.244 extracted from

  • Saa, L.; Jaureguibeitia, A.; Largo, E.; Llama, M.; Serra, J.
    Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1 (2010), Appl. Microbiol. Biotechnol., 86, 201-211 .
    View publication on PubMed
Search for more literature for 1.14.13.244

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rhodococcus erythropolis

Inhibitors

Inhibitors Comment Organism Structure
Co2+ 1 mM, 80% residual activity Rhodococcus erythropolis
Cu2+ 0.02 mM, no residual activity Rhodococcus erythropolis
Fe2+ 1 mM, 51% residual activity Rhodococcus erythropolis
Fe3+ 0.1 mM, 77% residual activity Rhodococcus erythropolis
N-ethylmaleimide 0.1 mM, 62% residual activity Rhodococcus erythropolis
Ni2+ 0.1 mM, 21% residual activity Rhodococcus erythropolis
p-hydroxymercuribenzoate 0.02 mM, no residual activity Rhodococcus erythropolis
Zn2+ 1 mM, 23% residual activity Rhodococcus erythropolis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0533
-
 NADH pH 6.8, 25°C Rhodococcus erythropolis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 1 mM, 127% of initial activity Rhodococcus erythropolis
Mn2+ 1 mM, 113% of initial activity Rhodococcus erythropolis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45000
-
 His-tagged subunit PheA2, gel filtration Rhodococcus erythropolis
236000
-
 His-tagged subunit PheA1, gel filtration Rhodococcus erythropolis
238000
-
 His-tagged subunit PheA1, PAGE Rhodococcus erythropolis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phenol + NADH + H+ + O2 Rhodococcus erythropolis
-
 catechol + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodococcus erythropolis A7LCL0 and A7LCL1 A7LCL0 i.e. subunit PheA1, A7LCL1 i.e subunit PheA2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenol + NADH + H+ + O2
-
 Rhodococcus erythropolis catechol + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
heteromer 4 * 60720, His-tagged subunit PheA1, 2 * 20350, His-tagged subunit PheA2, calculated from sequence. 4 * 62000, His-tagged subunit PheA1, 2 * 22000, His-tagged subunit PheA2, SDS-PAGE Rhodococcus erythropolis

Cofactor

Cofactor Comment Organism Structure
FAD Km value 0.0134 mM Rhodococcus erythropolis
NADH
-
 Rhodococcus erythropolis
NADPH activity is 5fold lower than with NADH Rhodococcus erythropolis

pI Value

Organism Comment pI Value Maximum pI Value
Rhodococcus erythropolis subunit PheA2, calculated from sequence
-
 5.2
Rhodococcus erythropolis subunit PheA1, calculated from sequence
-
 5.8

General Information

General Information Comment Organism
physiological function recombinant His6PheA1 exists as a homotetramer of four identical subunits of 62 kDa that has no phenol hydroxylase activity on its own. Recombinant His6PheA2 is a homodimeric flavin reductase, that uses NAD(P)H in order to reduce flavin adenine dinucleotide (FAD), according to a random sequential kinetic mechanism. The hydroxylation of phenol in vitro requires the presence of both His6PheA1 and His6PheA2 components, in addition to NADH and FAD, but the physical interaction between the proteins is not necessary for the reaction Rhodococcus erythropolis