Information on EC 5.3.99.7 - styrene-oxide isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.99.7
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RECOMMENDED NAME
GeneOntology No.
styrene-oxide isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
styrene oxide = phenylacetaldehyde
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Microbial metabolism in diverse environments
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Styrene degradation
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SYSTEMATIC NAME
IUBMB Comments
styrene-oxide isomerase (epoxide-cleaving)
Highly specific.
CAS REGISTRY NUMBER
COMMENTARY hide
124541-89-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
aerobic bacterium (strain S5)
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Manually annotated by BRENDA team
strain AC-5
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Manually annotated by BRENDA team
no activity in Rhodococcus sp. strain ST-10
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Manually annotated by BRENDA team
strain CA-3
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Manually annotated by BRENDA team
strain S12
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Manually annotated by BRENDA team
strain SN1
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Manually annotated by BRENDA team
strain SK3
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Manually annotated by BRENDA team
strain SK3
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene styC, strain ST-5 has a gene cluster containing four open reading frames which encode styrene degradation enzymes
UniProt
Manually annotated by BRENDA team
gene styC, strain ST-5 has a gene cluster containing four open reading frames which encode styrene degradation enzymes
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-styrene oxide
phenylacetaldehyde
show the reaction diagram
(R,S)-3-chlorostyrene oxide
3-chlorophenylacetaldehyde
show the reaction diagram
(R,S)-4-bromostyrene oxide
4-bromophenylacetaldehyde
show the reaction diagram
(R,S)-4-chlorostyrene oxide
4-chlorophenylacetaldehyde
show the reaction diagram
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low activity
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?
(R,S)-4-fluorostyrene oxide
4-fluorophenylacetaldehyde
show the reaction diagram
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-
-
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?
(R,S)-4-methylstyrene oxide
4-methylphenylacetaldehyde
show the reaction diagram
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-
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?
(R,S)-styrene oxide
phenylacetaldehyde
show the reaction diagram
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best substrate
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?
(S)-styrene oxide
phenylacetaldehyde
show the reaction diagram
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best substrate
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?
1a,2,3,7b-tetrahydronaphtho[1,2-b]oxirene
3,4-dihydronaphthalen-2(1H)-one
show the reaction diagram
2-(4-chlorophenyl)oxirane
(4-chlorophenyl)acetaldehyde
show the reaction diagram
2-(4-methylphenyl)oxirane
(4-methylphenyl)acetaldehyde
show the reaction diagram
2-ethyl-2-phenyloxirane
2-phenylbutanal
show the reaction diagram
2-methyl-2-phenyloxirane
hydratropaldehyde
show the reaction diagram
2-phenyloxirane
phenylacetaldehyde
show the reaction diagram
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?
6,6a-dihydro-1aH-indeno[1,2-b]oxirene
1,3-dihydro-2H-inden-2-one
show the reaction diagram
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45% of the activity with 2-phenyloxirane
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?
styrene oxide
phenylacetaldehyde
show the reaction diagram
styrene oxide + H2O
phenylacetaldehyde
show the reaction diagram
additional information
?
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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
styrene oxide
phenylacetaldehyde
show the reaction diagram
styrene oxide + H2O
phenylacetaldehyde
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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non-metal enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AgNO3
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0.1 mM, 29% inhibition
dithiothreitol
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1 mM, 22% inhibition
HgCl2
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1 mM, 80% inhibition
hydrazine
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1 mM, 82% inhibition
hydroxylammonium chloride
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1 mM, 77% inhibition
iodoacetate
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1 mM, 80% inhibition
KCN
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1 mM, 32% inhibition
PCMB
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1 mM, 24% inhibition
phenylacetaldehyde
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irreversible product inhibition, half-life of 15 min determined at a phenylacetaldehyde concentration of about 55 mM
Tris hydrochloride
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.077
styrene oxide
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pH 7.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.12
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styrene-grown cell extract, pH 7.2, 22°C
42.1
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partially purified enzyme, pH 7.2, 22°C
91.7
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partially purified enzyme, pH 7.2, 65°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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pH 5.0-7.5: maximal activity, pH 10.0: about 50% of maximal activity
additional information
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wide pH tolerance
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
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activity range, wide temperature tolerance, profile overview
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
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25°C, 1 h, unstable below
648825
7 - 8
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25°C, 1 h
648825
7
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partially purified native enzyme, 30 min, most stable at
726724
10
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25°C, 1 h, 10% loss of activity
648825
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
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partially purified native enzyme, 30 min, most stable at
40
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pH 7.0, 1 h, stable
50
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pH 7.0, 1 h, 10% loss of activity
55
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pH 7.0, 1 h, 50% loss of activity
60
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pH 7.0, 1 h, 80% loss of activity
65
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partially purified native enzyme, 30 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 50 mM potassium phosphate buffer, pH 7.0, 30% loss of activity after 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme partially from styrene-grown cells by membrane preparation and solubilization
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene styC, DNA and amino acid sequence determination and analysis, genetic organization, expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is strongly induced by styrene, to a lesser extent by styrene oxide and phenylacetaldehyde, no induction by phenylacetic acid or glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis