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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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
LITERATURE
1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-hydroxypentalenate + succinate + CO2
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
neopentalenoketolactone and pentalenate biosynthesis
-
-
pentalenolactone biosynthesis
-
-
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.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
COMMENTARY
LITERATURE
Iron
-
non-heme iron, alpha-ketoglutarate-dependent hydroxylase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.57
(+/-)-1-deoxypentalenic acid
-
pH 6.0, temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.2
(+/-)-1-deoxypentalenic acid
-
pH 6.0, temperature not specified in the publication
-
pH OPTIMUM
ORGANISM
UNIPROT
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
COMMENTARY
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R117Q
-
complete loss of activity
R188Q
-
280fold decrease in activity