Information on EC 5.3.3.19 - 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase

for references in articles please use BRENDA:EC5.3.3.19
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Bacillus subtilis group

EC NUMBER
COMMENTARY hide
5.3.3.19
-
RECOMMENDED NAME
GeneOntology No.
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate = 3-[(1E,4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
bacilysin biosynthesis
Biosynthesis of antibiotics
-
-
SYSTEMATIC NAME
IUBMB Comments
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate isomerase
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme can interconvert the (E) isomer formed in the reaction into the (Z) isomer [2], although this isomerization is not part of the pathway leading to bacilysin [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
disruption of bacB, the gene in the cluster responsible for synthesizing bacilysin abolishes the bactericidal activity of Bacillus amyloliquefaciens FZB42 against Microcystis aeruginosa
metabolism
the enzyme is involved in the bacilysin biosynthetic pathway
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
(3E)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
show the reaction diagram
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
show the reaction diagram
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
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
(3Z)-3-[(4R)-4-hydroxycyclohex-2-en-1-ylidene]-2-oxopropanoate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
formation of the the 3Z isomer is severely inhibited by high concentrations of salt (above 250 mM)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.423
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
-
pH 8.1, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.52
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate
-
pH 8.1, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
8.1
-
assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BacB can be crystallized in three different crystal forms by slight modification of the crystallization conditions. The concentration of 2,4-methylpentanediol substantially influences crystallization
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable without glycerol in storage buffer
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE