Literature summary for 1.4.3.5 extracted from

Di Salvo, M.; Yang, E.; Zhao, G.; Winkler, M.E.; Schirch, V.
Expression, purification, and characterization of recombinant Escherichia coli pyridoxine 5'-phosphate oxidase (1998), Protein Expr. Purif., 13, 349-356.

Search for more literature for 1.4.3.5

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.002	-	pyridoxine 5'-phosphate	-	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
28000	-	2 * 28000, SDS-PAGE	Escherichia coli
51000	-	-	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.293	-	recombinant enzyme	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyridoxamine 5'-phosphate + H2O + O2	-	Escherichia coli	pyridoxal 5'-phosphate + NH3 + H2O2	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 28000, SDS-PAGE	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.2	-	pyridoxine 5'-phosphate	recombinant enzyme, in phosphate and HEPES buffer at pH 7.6	Escherichia coli
0.3	-	pyridoxine 5'-phosphate	recombinant enzyme, in Tris buffer at pH 7.6	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
FMN	2 molecules of FMN bound per homodimer	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)