Information on EC 1.14.11.35 - 1-deoxypentalenic acid 11beta-hydroxylase

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The expected taxonomic range for this enzyme is: Streptomyces avermitilis

EC NUMBER
COMMENTARY
1.14.11.35
-
RECOMMENDED NAME
GeneOntology No.
1-deoxypentalenic acid 11beta-hydroxylase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + succinate + CO2
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
neopentalenoketolactone and pentalenate biosynthesis
-
pentalenolactone biosynthesis
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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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pntH
-
-
gene name
-
ptlH
-
-
gene name
-
ptlH
Q82IZ1
gene name
sav2991
-
-
gene name
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-1-deoxypentalenic acid + O2
11beta-hydroxy-1-deoxypentalenic acid + succinate + CO2
show the reaction diagram
Q82IZ1
-
-
-
?
additional information
?
-
Q82IZ1
no substrate: (+/-)-pentalenene, (+/-)-pentalen-13-ol
-
-
-
additional information
?
-
-
no substrate: ent-1-deoxypentalenic acid
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Iron
-
non-heme iron, alpha-ketoglutarate-dependent hydroxylase
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.57
-
(+/-)-1-deoxypentalenic acid
-
pH 6.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.2
-
(+/-)-1-deoxypentalenic acid
-
pH 6.0, temperature not specified in the publication
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 37121, calculated, x * 37139, MALDI-TOF
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
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Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R117Q
-
complete loss of activity
R188Q
-
280fold decrease in activity