PDBsum entry 4fcs

Oxidoreductase

PDB id

4fcs

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Contents

			Protein chain

					315 a.a.

			Ligands

					HEM


					SO4


					GOL ×2

			Metals

					_CA ×2

			Waters ×363

PDB id:

4fcs

Links

Name:

Oxidoreductase

Title:

The crystal structures of several mutants of pleurotus eryngii versatile peroxidase

Structure:

Versatile peroxidase vpl2. Chain: a. Fragment: unp residues 31-349. Synonym: versatile liquid phase peroxidase 2. Engineered: yes. Mutation: yes

Source:

Pleurotus eryngii. Boletus of the steppes. Organism_taxid: 5323. Gene: vpl2. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.50Å

R-factor:

0.151

R-free:

0.176

Authors:

M.J.Mate,A.Romero,F.J.Ruiz-Duenas,A.T.Martinez

Key ref:

M.Morales et al. (2012). Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase. J Biol Chem, 287, 41053-41067. PubMed id: 23071108

Date:

25-May-12

Release date:

24-Oct-12

PROCHECK

	Headers

	References

Protein chain

O94753 (VPL2_PLEER) - Versatile peroxidase VPL2 from Pleurotus eryngii

Seq: Struc:					361 a.a. 315 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.1.11.1.16 - versatile peroxidase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

1.	1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = guaiacol + vanillin + glycolaldehyde + H2O
2.	2 Mn²⁺ + H2O2 + 2 H⁺ = 2 Mn³⁺ + 2 H2O

1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol

H2O2

guaiacol
Bound ligand (Het Group name = GOL)
matches with 66.67% similarity

vanillin

glycolaldehyde

H2O

2 × Mn(2+)	+	H2O2	+	2 × H(+)	=	2 × Mn(3+)	+	2 × H2O

Cofactor:

Heme

Heme
Bound ligand (Het Group name = HEM) matches with 95.45% similarity

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

	J Biol Chem 287:41053-41067 (2012)
PubMed id: 23071108

Two oxidation sites for low redox potential substrates: a directed mutagenesis, kinetic, and crystallographic study on Pleurotus eryngii versatile peroxidase.
M.Morales, M.J.Mate, A.Romero, M.J.Martínez, �.�.T.Martínez, F.J.Ruiz-Dueñas.

ABSTRACT

No abstract given.