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Information on EC 3.7.1.22 - 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (ring-opening) and Organism(s) Bacillus subtilis and UniProt Accession P42415

for references in articles please use BRENDA:EC3.7.1.22
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IUBMB Comments
The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol degradation pathway leading to acetyl-CoA.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P42415
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
IolD, More, THcHDO hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
THcHDO hydrolase
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SYSTEMATIC NAME
IUBMB Comments
D-3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (ring-opening)
The enzyme, found in the bacterium Bacillus subtilis, is part of the myo-inositol degradation pathway leading to acetyl-CoA.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3D-3,5/4-trihydroxycyclohexa-1,2-dione + H2O
5-deoxy-D-glucuronate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3D-3,5/4-trihydroxycyclohexa-1,2-dione + H2O
5-deoxy-D-glucuronate
show the reaction diagram
the enzyme is part of the myo-inositol degradation pathway leading to acetyl-CoA
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
253
protein extract of Escherichia coli cells that recombinantly express the enzyme, pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is part of the myo-inositol degradation pathway leading to acetyl-CoA
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, K., Yamaguchi, M.; Morinaga, T.; Kinehara, M.; Ikeuchi, M.; Ashida, H.; Fujita, Y.
myo-Inositol catabolism in Bacillus subtilis
J. Biol. Chem.
283
10415-10424
2008
Bacillus subtilis (P42415), Bacillus subtilis 168 (P42415)
Manually annotated by BRENDA team