Novel phacB-encoded cytochrome P450 monooxygenase from Aspergillus nidulans with 3-hydroxyphenylacetate 6-hydroxylase and 3,4-dihydroxyphenylacetate 6-hydroxylase activities

Ferrer-Sevillano, F.; Fernandez-Canon, J.M.; Eukaryot. Cell 6, 514-520 (2007)

Data extracted from this reference:

Activating Compound

Activating Compound	Commentary	Organism	Structure
additional information	phenylacetate and its hydroxyderivatives strongly induce the enzyme	Emericella nidulans	-

Cloned(Commentary)

Commentary	Organism
DNA and amino acid sequence determination and analysis, expression pattern, sequence comparison, expression in a recombinant Aspergillus nidulans strain	Emericella nidulans

Engineering

Amino acid exchange	Commentary	Organism
additional information	a phacB-disrupted strain DELTAphacB does not grow on 3-hydroxy-, 4-hydroxy-, or 3,4-dihydroxy-phenylacetate, overview	Emericella nidulans

Metals/Ions

Metals/Ions	Commentary	Organism	Structure
Fe2+	the enzyme is a cytochrome P450 monooxygenase containing a heme iron	Emericella nidulans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Commentary (Nat. Sub.)	Natural Products	Commentary (Nat. Pro.)	Organism (Nat. Pro.)	Reversibility
2-hydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	?

Organism

Organism	Primary Accession No. (UniProt)	Commentary	Textmining
Emericella nidulans	Q078T0	strain BiA1, gene phacB	-
Emericella nidulans BiA1	Q078T0	strain BiA1, gene phacB	-

Source Tissue

Source Tissue	Commentary	Organism	Textmining
mycelium	-	Emericella nidulans	-

Substrates and Products (Substrate)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
2-hydroxyphenylacetate + NAD(P)H + O2	low activity	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
2-hydroxyphenylacetate + NAD(P)H + O2	low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	-	673422	Emericella nidulans	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	-	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Commentary	Organism
37	-	assay at	Emericella nidulans

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Commentary	Organism
7	-	assay at	Emericella nidulans

Cofactor

Cofactor	Commentary	Organism	Structure
NADH	-	Emericella nidulans
NADPH	-	Emericella nidulans

Activating Compound (protein specific)

Activating Compound	Commentary	Organism	Structure
additional information	phenylacetate and its hydroxyderivatives strongly induce the enzyme	Emericella nidulans	-

Cloned(Commentary) (protein specific)

Commentary	Organism
DNA and amino acid sequence determination and analysis, expression pattern, sequence comparison, expression in a recombinant Aspergillus nidulans strain	Emericella nidulans

Cofactor (protein specific)

Cofactor	Commentary	Organism	Structure
NADH	-	Emericella nidulans
NADPH	-	Emericella nidulans

Engineering (protein specific)

Amino acid exchange	Commentary	Organism
additional information	a phacB-disrupted strain DELTAphacB does not grow on 3-hydroxy-, 4-hydroxy-, or 3,4-dihydroxy-phenylacetate, overview	Emericella nidulans

Metals/Ions (protein specific)

Metals/Ions	Commentary	Organism	Structure
Fe2+	the enzyme is a cytochrome P450 monooxygenase containing a heme iron	Emericella nidulans

Natural Substrates/ Products (Substrates) (protein specific)

Natural Substrates	Organism	Commentary (Nat. Sub.)	Natural Products	Commentary (Nat. Pro.)	Organism (Nat. Pro.)	Reversibility
2-hydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	Emericella nidulans	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	?

Source Tissue (protein specific)

Source Tissue	Commentary	Organism	Textmining
mycelium	-	Emericella nidulans	-

Substrates and Products (Substrate) (protein specific)

Substrates	Commentary Substrates	Literature (Substrates)	Organism	Products	Commentary (Products)	Literature (Products)	Organism (Products)	Reversibility
2-hydroxyphenylacetate + NAD(P)H + O2	low activity	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
2-hydroxyphenylacetate + NAD(P)H + O2	low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	-	673422	Emericella nidulans	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3,4-dihydroxyphenylacetate + NAD(P)H + O2	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	-	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	-	-	-	?
3-hydroxyphenylacetate + NAD(P)H + O2	step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview	673422	Emericella nidulans	2,5-dihydroxyphenylacetate + NAD(P)+ + H2O	the product is a substrate for homogentisate dioxygenase	-	-	?

Temperature Optimum [°C] (protein specific)

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Commentary	Organism
37	-	assay at	Emericella nidulans

pH Optimum (protein specific)

pH Optimum Minimum	pH Optimum Maximum	Commentary	Organism
7	-	assay at	Emericella nidulans

See also following references to EC number 1.14.13.63 (sorted by year of publication):

No.	1st author	Pub Med	title	organims	journal	volume	pages	year	Activating Compound	Application	Cloned(Commentary)	Crystallization (Commentary)	Engineering	General Stability	Inhibitors	KM Value [mM]	Localization	Metals/Ions	Molecular Weight [Da]	Natural Substrates/ Products (Substrates)	Organic Solvent Stability	Organism	Oxidation Stability	Posttranslational Modification	Purification (Commentary)	Reaction	Renatured (Commentary)	Source Tissue	Specific Activity [micromol/min/mg]	Storage Stability	Substrates and Products (Substrate)	Subunits	Temperature Optimum [°C]	Temperature Range [°C]	Temperature Stability [°C]	Turnover Number [1/s]	pH Optimum	pH Range	pH Stability	Cofactor	Ki Value [mM]	pI Value	IC50 Value	Activating Compound (protein specific)	Application (protein specific)	Cloned(Commentary) (protein specific)	Cofactor (protein specific)	Crystallization (Commentary) (protein specific)	Engineering (protein specific)	General Stability (protein specific)	IC50 Value (protein specific)	Inhibitors (protein specific)	Ki Value [mM] (protein specific)	KM Value [mM] (protein specific)	Localization (protein specific)	Metals/Ions (protein specific)	Molecular Weight [Da] (protein specific)	Natural Substrates/ Products (Substrates) (protein specific)	Organic Solvent Stability (protein specific)	Oxidation Stability (protein specific)	Posttranslational Modification (protein specific)	Purification (Commentary) (protein specific)	Renatured (Commentary) (protein specific)	Source Tissue (protein specific)	Specific Activity [micromol/min/mg] (protein specific)	Storage Stability (protein specific)	Substrates and Products (Substrate) (protein specific)	Subunits (protein specific)	Temperature Optimum [°C] (protein specific)	Temperature Range [°C] (protein specific)	Temperature Stability [°C] (protein specific)	Turnover Number [1/s] (protein specific)	pH Optimum (protein specific)	pH Range (protein specific)	pH Stability (protein specific)	pI Value (protein specific)	Expression	General Information	General Information (protein specific)	Expression (protein specific)	KCat/KM [mM/s]	KCat/KM [mM/s] (protein specific)
673422	Ferrer-Sevillano		Novel phacB-encoded cytochrome ...	Emericella nidulans	Eukaryot. Cell	6	514-520	2007	1	-	1	-	1	-	-	-	-	1	-	3	-	5	-	-	-	-	-	1	-	-	6	-	1	-	-	-	1	-	-	2	-	-	-	1	-	1	2	-	1	-	-	-	-	-	-	1	-	3	-	-	-	-	-	1	-	-	6	-	1	-	-	-	1	-	-	-	-	-	-	-	-	-
659614	Suemori	-	Purification and characterizat ...	Rhodococcus erythropolis	J. Ferment. Bioeng.	81	133-137	1996	-	-	-	-	-	-	-	-	-	-	2	1	-	2	-	-	1	-	-	-	1	-	3	1	-	-	-	-	-	-	-	3	-	-	-	-	-	-	3	-	-	-	-	-	-	-	-	-	2	1	-	-	-	1	-	-	1	-	3	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-
7425	van Berkel		Purification and characterisat ...	Flavobacterium sp.	Eur. J. Biochem.	201	585-591	1991	-	-	-	-	-	1	5	4	-	-	1	-	-	6	-	-	1	-	-	1	1	1	6	1	-	-	-	4	1	1	2	1	-	-	-	-	-	-	1	-	-	1	-	5	-	4	-	-	1	-	-	-	-	1	-	1	1	1	6	1	-	-	-	4	1	1	2	-	-	-	-	-	-	-
7426	Van den Tweel	-	Catabolism of DL-alpha-phenylh ...	Flavobacterium sp.	Arch. Microbiol.	149	207-213	1988	-	-	-	-	-	-	-	-	-	-	-	1	-	1	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	1	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-