KEGG ENZYME: 1.14.11.35

ENZYME: 1.14.11.35

Entry

EC 1.14.11.35               Enzyme

Name

1-deoxypentalenic acid 11beta-hydroxylase;
ptlH (gene name);
sav2991 (gene name);
pntH (gene name)

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

Sysname

1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase

Reaction(IUBMB)

1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + succinate + CO2 [RN:R10157]

Reaction(KEGG)

R10157

Substrate

1-deoxypentalenate [CPD:C20404];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]

Product

1-deoxy-11beta-hydroxypentalenate [CPD:C20403];
succinate [CPD:C00042];
CO2 [CPD:C00011]

Comment

The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.

History

EC 1.14.11.35 created 2012

Pathway

ec00998

Biosynthesis of various antibiotics

ec01100

Metabolic pathways

ec01110

Biosynthesis of secondary metabolites

Orthology

K18056

1-deoxypentalenic acid 11beta-hydroxylase

Genes

ADY:	HLG70_10405

SMA:	SAVERM_2991(ptlH)

SBH:

SBI_09673

SCI:	B446_29665

SCW:	TU94_27375

SLE:	sle_13220(sle_13220)

SSIA:

A7J05_09270

SGJ:	IAG43_27125

SHK:	J2N69_35835

DSN:	HWI92_19215

Reference

1 [PMID:16704250]

Authors

You Z, Omura S, Ikeda H, Cane DE

Title

Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis.

Journal

J Am Chem Soc 128:6566-7 (2006)
DOI:10.1021/ja061469i

Sequence

[sma:SAVERM_2991]

Reference

2 [PMID:17942405]

Authors

You Z, Omura S, Ikeda H, Cane DE, Jogl G

Title

Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis.

Journal

J Biol Chem 282:36552-60 (2007)
DOI:10.1074/jbc.M706358200