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Information on EC 1.3.3.10 - tryptophan alpha,beta-oxidase
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1.3.3.10 tryptophan alpha,beta-oxidaseIUBMB Comments
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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The enzyme appears in viruses and cellular organisms
Synonyms
EC 1.4.3.17, L-tryptophan 2',3'-oxidase, L-tryptophan alpha,beta-dehydrogenase, LTO, tryptophan side chain oxidase II, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.4.3.17
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-
formerly
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L-tryptophan 2',3'-oxidase
L-tryptophan alpha,beta-dehydrogenase
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LTO
L-tryptophan 2',3'-oxidase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + O2 = alpha,beta-didehydrotryptophan + H2O2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
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-
-
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reduction
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-
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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
156859-19-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pentagastrin + O2
N-[(2E)-2-{[N-(tert-butoxycarbonyl)-beta-alanyl]amino}-3-(1H-indol-3-yl)prop-2-enoyl]-L-methionyl-L-alpha-aspartyl-L-phenylalaninamide + H2O2
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-
-
?
tryptophan No.14 of alpha-globin + O2
alpha,beta-dehydrotryptophan + H2O2
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-
-
?
tryptophan No.15 of beta-globin + O2
alpha,beta-dehydrotryptophan + H2O2
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-
-
?
calcium-dependent lipopeptide antibiotic + O2
? + H2O2
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-
-
-
?
L-tryptophan + O2
alpha,beta-didehydrotryptophan + H2O2
-
-
-
?
L-tryptophan + O2
alpha,beta-didehydrotryptophan + H2O2
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-
-
?
L-tryptophanamide + O2
alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
L-tryptophanamide + O2
alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
N-acetyl-L-tryptophan + O2
N-acetyl-alpha,beta-didehydrotryptophan + H2O2
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-
-
?
N-acetyl-L-tryptophan + O2
N-acetyl-alpha,beta-didehydrotryptophan + H2O2
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O2
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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NAD+, NADP+, FAD, or FMN show no effect on the activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no inhibition with L-histidine, N-acetyl-L-phenylalaninamide and N-acetyl-L-tyrosinamide
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additional information
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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
LITERATURE
IMAGE
0.93
adrenocorticotropic hormone
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dehydrogenation of the tryptophanyl side chain
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0.071
Luteinizing hormone-releasing hormone
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dehydrogenation of the tryptophanyl side chain
0.026
pentagastrin
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dehydrogenation of the tryptophanyl side chain
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.283
adrenocorticotropic hormone
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dehydrogenation of the tryptophanyl side chain
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0.333
Luteinizing hormone-releasing hormone
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dehydrogenation of the tryptophanyl side chain
0.533
pentagastrin
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dehydrogenation of the tryptophanyl side chain
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
octamer
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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
octamer
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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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takai, K.; Sasai, Y.; Morimoto, H.; Yamazaki, H.; Yoshii, H.; Inoue, S.
Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II
J. Biol. Chem.
259
4452-4457
1984
Pseudomonas sp.
brenda
Ito, S.; Takai, K.; Tokuyama, T.; Hayaishi, O.
Enzymatic modification of tryptophan residues by tryptophan side chain oxidase I and II from Pseudomonas
J. Biol. Chem.
256
7834-7843
1981
Pseudomonas sp.
brenda
Genet, R.; Benetti, P.H.; Hammadi, A.; Menez, A.
L-tryptophan 2',3'-oxidase from Chromobacterium violaceum
J. Biol. Chem.
270
23540-23545
1995
Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472
brenda
Genet, R.; Donoyelle, C.; Menez, A.
Purification and partial characterization of an amino acid alpha,beta-dehydrogenase, L-tryptophan 2',3'-oxidase from Chromobacterium violaceum
J. Biol. Chem.
269
18177-18184
1994
Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472
brenda
Amir-Heidari, B.; Thirlway, J.; Micklefield, J.
Stereochemical course of tryptophan dehydrogenation during biosynthesis of the calcium-dependent lipopeptide antibiotics
Org. Lett.
9
1513-1516
2007
Streptomyces coelicolor, Streptomyces coelicolor WH101.10
brenda
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