Information on EC 1.3.3.10 - tryptophan alpha,beta-oxidase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.3.3.10
-
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RECOMMENDED NAME
GeneOntology No.
tryptophan alpha,beta-oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + O2 = alpha,beta-didehydrotryptophan + H2O2
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:oxygen alpha,beta-oxidoreductase
Requires heme. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Also catalyses the alpha,beta dehydrogenation of L-tryptophan side chains in peptides. The product of the reaction can hydrolyse spontaneously to form (indol-3-yl)pyruvate.
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CAS REGISTRY NUMBER
COMMENTARY hide
156859-19-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC12472
-
-
Manually annotated by BRENDA team
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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
adrenocorticotropic hormone + O2
? + H2O2
show the reaction diagram
-
-
-
?
calcium-dependent lipopeptide antibiotic + O2
? + H2O2
show the reaction diagram
indole-3-propionate + O2
? + H2O2
show the reaction diagram
L-tryptophan + O2
alpha,beta-didehydrotryptophan + H2O2
show the reaction diagram
L-tryptophanamide + O2
alpha,beta-didehydrotryptophanamide + H2O2
show the reaction diagram
luteinizing hormone-releasing hormone + O2
? + H2O2
show the reaction diagram
-
-
-
?
N-acetyl-L-tryptophan + O2
N-acetyl-alpha,beta-didehydrotryptophan + H2O2
show the reaction diagram
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O2
show the reaction diagram
pentagastrin + O2
? + H2O2
show the reaction diagram
-
-
-
?
tryptophan No.14 of alpha-globin + O2
alpha,beta-dehydrotryptophan + H2O2
show the reaction diagram
-
-
-
?
tryptophan No.15 of beta-globin + O2
alpha,beta-dehydrotryptophan + H2O2
show the reaction diagram
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
NAD+, NADP+, FAD, or FMN show no effect on the activity
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
-
10 mM, residual activity 103%
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-hydroxy-L-tryptophan
D-tryptophan
methyl-3-indole
Sodium dodecyl sulfate
-
no modification with 0.4% SDS
tryptamine
Urea
-
no modification with 8 M urea
additional information
-
no inhibition with L-histidine, N-acetyl-L-phenylalaninamide and N-acetyl-L-tyrosinamide
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.93
adrenocorticotropic hormone
-
dehydrogenation of the tryptophanyl side chain
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0.02
indole-3-propionate
-
-
0.0058
L-tryptophan
-
-
0.0091
L-Tryptophanamide
-
-
0.071
Luteinizing hormone-releasing hormone
-
dehydrogenation of the tryptophanyl side chain
0.0791
N-acetyl-L-tryptophan
-
-
0.0195
N-Acetyl-L-tryptophanamide
-
-
0.026
pentagastrin
-
dehydrogenation of the tryptophanyl side chain
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.283
adrenocorticotropic hormone
-
dehydrogenation of the tryptophanyl side chain
-
0.785
indole-3-propionate
-
-
0.66
L-tryptophan
-
-
0.593
L-Tryptophanamide
-
-
0.333
Luteinizing hormone-releasing hormone
-
dehydrogenation of the tryptophanyl side chain
0.79
N-acetyl-L-tryptophan
-
-
0.753
N-Acetyl-L-tryptophanamide
-
-
0.533
pentagastrin
-
dehydrogenation of the tryptophanyl side chain
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
5-hydroxy-L-tryptophan
-
-
0.0066
D-tryptophan
-
-
0.0013
methyl-3-indole
-
-
0.0054
tryptamine
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
substrate tryptophanamide
0.07
-
substrate tryptophan-leucine
0.31
-
substrate tryptophan
0.74
-
substrate leucin-tryptophan-leucin
1.08
-
substrate indolepropionic acid
1.42
-
substrate N-acetyltryptophanamide
1.82
-
substrate N-acetyltryptophan
2.32
-
substrate leucin-tryptophan
30.3
-
after purification
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
alpha, 4 * 14000 + beta 4 * 74000, organized in an alpha4,beta4 manner, heterooligomeric structure, one heme molecule per alpha,beta protomer, SDS-PAGE
74000
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alpha, 4 * 14000 + beta 4 * 74000, organized in an alpha4,beta4 manner, heterooligomeric structure, one heme molecule per alpha,beta protomer, SDS-PAGE
150000
-
-
680000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
after dilution in 0.1 M bis-Tris buffer
639382
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
-
active up to 80øC
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active with 0.2 M dithiothreitol, 1% SDS, or 4.5 M urea
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, for several months and for 24-48 h at room temperature in the absence of any additives
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cell disruption with Eaton press, ultracentrifugation, ammonium sulfate precipitation, DEAE-column, concentration using centrifugal microcentrators, gel filtration, purified 108fold, yield 33.8%
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gel filtration, phosphocellulose column chromatography, SDS-PAGE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.3.10)
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)