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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.11.1.16

Accepted Name
Versatile peroxidase.
Alternative Name(s)
Hybrid peroxidase.
Polyvalent peroxidase.
VP.
Reaction catalysed
  • 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H(2)O(2) <=> 4-hydroxy-3-methoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H(2)O
  • 2 manganese(II) + 2 H(+) + H(2)O(2) <=> 2 manganese(III) + 2 H(2)O
Cofactor(s)
Heme.
Comment(s)
  • This ligninolytic peroxidase combines the substrate-specificity characteristics of the two other ligninolytic peroxidases, EC 1.11.1.13 and EC 1.11.1.14.
  • Unlike these two enzymes, it is also able to oxidize phenols, hydroquinones and both low- and high-redox-potential dyes, due to a hybrid molecular architecture that involves multiple binding sites for substrates.
Cross-references
PROSITEPDOC00394
BRENDA1.11.1.16
EC2PDB1.11.1.16
ExplorEnz1.11.1.16
PRIAM enzyme-specific profiles1.11.1.16
KEGG Ligand Database for Enzyme Nomenclature1.11.1.16
IUBMB Enzyme Nomenclature1.11.1.16
IntEnz1.11.1.16
MEDLINEFind literature relating to 1.11.1.16
MetaCyc1.11.1.16
UniProtKB/Swiss-Prot
K7N5M8, DYP2_AMYS7;  Q9UR19, VPL1_PLEER;  O94753, VPL2_PLEER;  
Q9UVP6, VPS1_PLEER;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.11.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.11.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-