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Information on EC 1.14.11.35 - 1-deoxypentalenic acid 11beta-hydroxylase and Organism(s) Streptomyces avermitilis and UniProt Accession Q82IZ1

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IUBMB Comments
The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
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Streptomyces avermitilis
UNIPROT: Q82IZ1
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The taxonomic range for the selected organisms is: Streptomyces avermitilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
pntH, ptlH, sav2991, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pntH
-
-
-
-
ptlH
-
-
-
-
sav2991
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
1-deoxypentalenic acid,2-oxoglutarate:oxygen oxidoreductase
The enzyme requires Fe(II) and ascorbate. Isolated from the bacterium Streptomyces avermitilis. Part of the pathway for pentalenolactone biosynthesis.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-1-deoxypentalenic acid + O2
11beta-hydroxy-1-deoxypentalenic acid + succinate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
non-heme iron, alpha-ketoglutarate-dependent hydroxylase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.57
(+/-)-1-deoxypentalenic acid
pH 6.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.2
(+/-)-1-deoxypentalenic acid
pH 6.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37121
x * 37121, calculated, x * 37139, MALDI-TOF
37139
x * 37121, calculated, x * 37139, MALDI-TOF
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37121, calculated, x * 37139, MALDI-TOF
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexes with the cofactors iron, alpha-ketoglutarate, and the nonreactive enantiomer of the substrate, ent-1-deoxypentalenic acid, in four different crystal forms to up to 1.31 A resolution. The overall structure of PtlH forms a double-stranded barrel helix fold and the cofactor-binding site for iron and alpha-keto-glutarate is similar to other double-stranded barrel helix fold enzymes. Binding of the substrate enantiomer induces a reorganization of the monoclinic crystal lattice leading to a disorder-order transition of a C-terminal alpha-helix. The newly formed helix blocks the major access to the active site and effectively traps the bound substrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R117Q
complete loss of activity
R188Q
280fold decrease in activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.
Pentalenolactone biosynthesis. Molecular cloning and assignment of biochemical function to PtlH, a non-heme iron dioxygenase of Streptomyces avermitilis
J. Am. Chem. Soc.
128
6566-6567
2006
Streptomyces avermitilis (Q82IZ1)
Manually annotated by BRENDA team
You, Z.; Omura, S.; Ikeda, H.; Cane, D.E.; Jogl, G.
Crystal structure of the non-heme iron dioxygenase PtlH in pentalenolactone biosynthesis
J. Biol. Chem.
282
36552-36560
2007
Streptomyces avermitilis (Q82IZ1)
Manually annotated by BRENDA team