Information on EC 1.13.99.1 - inositol oxygenase and Organism(s) Homo sapiens and UniProt Accession Q9UGB7

for references in articles please use BRENDA:EC1.13.99.1
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This record set is specific for:
Homo sapiens
UNIPROT: Q9UGB7


The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.13.99.1
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RECOMMENDED NAME
GeneOntology No.
inositol oxygenase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
myo-Inositol + O2 = D-glucuronate + H2O
show the reaction diagram
the N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
UDP-alpha-D-glucuronate biosynthesis (from myo-inositol)
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Ascorbate and aldarate metabolism
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Inositol phosphate metabolism
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SYSTEMATIC NAME
IUBMB Comments
myo-Inositol:oxygen oxidoreductase
An iron protein.
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CAS REGISTRY NUMBER
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9029-59-8
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ORGANISM
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LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
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LITERATURE
metabolism
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MIOX is the first and rate-limiting enzyme in myo-inositol metabolism pathway
additional information
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increase in MIOX enzyme activity is in proportion to serum glucose concentrations and may be responsible for the myo-inositol depletion found in the type I diabetes mellitus complications, detailed phenotype analysis of 130 Caucasian patients, overview
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myo-inositol + O2
D-glucuronic acid + H2O
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
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LITERATURE
Iron
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diiron cluster
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INHIBITORS
ORGANISM
UNIPROT
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LITERATURE
IMAGE
6-(4-hydroxy-3,5-dimethoxyphenyl)-4,8-dihydronaphthalene-1,3,8-triol
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docking energy level (Kcal/mol): -6.9602
ascochitine
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docking energy level (Kcal/mol): -9.5382
heritonin
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docking energy level (Kcal/mol): -10.4072
stigmasterol
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docking energy level (Kcal/mol): -14.589
taraxasterol
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docking energy level (Kcal/mol): -14.8894
tretinoin
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docking energy level (Kcal/mol): -12.1034
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5 - 5.8
myo-inositol
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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is expressed at low levels in cell types where diabetic complications occur
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
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1 * 33000, deduced from nucleotide sequence, SDS-PAGE
33000
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SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 33000, deduced from nucleotide sequence, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with myo-inosose-1 bound in a terminal mode to the enzyme's diiron cluster site. The N-terminus is important, through coordination of a set of loops covering the active site, in shielding the active site during catalysis. Role of residue K127 in governing the access o the diiron cluster
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after storage at 4�C for few weeks, a specific truncation due to degradation is observed, extended storage also causes the accumulation of a small proportion of apparantly dimerized MIOX
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant MIOX
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in epithelial cell line LLC-PK1
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expression in Escherichia coli
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genotyping of MIOX in Caucasian type I diabetes mellitus patients, overview
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LINKS TO OTHER DATABASES (specific for EC-Number 1.13.99.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)