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

ec01130

Biosynthesis of antibiotics

Orthology

K18056

1-deoxypentalenic acid 11beta-hydroxylase

Genes

SMA:	SAV_2991(ptlH)
SBH:	SBI_09673
SCI:	B446_29665
SCW:	TU94_27375

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 (2006) 6566-7.

Sequence

[sma:SAV_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 (2007) 36552-60.