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Information on EC 4.3.3.1 - 3-ketovalidoxylamine C-N-lyase
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4.3.3.1 3-ketovalidoxylamine C-N-lyaseIUBMB Comments
Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-alpha-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.
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Word Map
- 4.3.3.1
- saccharophilum
-
flavobacterium
- stenotrophomonas
-
pseudo-first
-
ethylenediaminetetraacetic
-
half-time
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
3-ketovalidoxylamine a c-n lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketovalidoxylamine A C-N lyase
lyase, 3-ketovalidoxylamine A C-N-
-
-
-
-
p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase
-
-
-
-
3-ketovalidoxylamine A C-N lyase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase [5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one-forming]
Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-alpha-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum.
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CAS REGISTRY NUMBER
COMMENTARY
99889-98-2
-
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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
3-ketovalidoxylamine A
(1S,2S,3R,6S)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol + (5R,6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
3-ketovalidoxylamine A
(6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohexa-2,4-dien-1-one + (1R,2S,3S,4R,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol
4-nitrophenyl-3-keto-validamine
4-nitroaniline + ?
-
assay at pH 7.0, 40°C
-
-
?
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
-
-
-
-
?
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + ?
-
assay at pH 7.0
-
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
3-ketovalidoxylamine A
(1S,2S,3R,6S)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol + (5R,6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
DI109203
-
i.e. valienamine
-
?
3-ketovalidoxylamine A
(1S,2S,3R,6S)-6-amino-4-(hydroxymethyl)cyclohex-4-ene-1,2,3-triol + (5R,6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohex-2-en-1-one
DI109203
-
i.e. valienamine
-
?
3-ketovalidoxylamine A
(6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohexa-2,4-dien-1-one + (1R,2S,3S,4R,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol
DI109203
-
i.e. validamine
-
?
3-ketovalidoxylamine A
(6R)-2,6-dihydroxy-5-(hydroxymethyl)cyclohexa-2,4-dien-1-one + (1R,2S,3S,4R,6R)-4-amino-6-(hydroxymethyl)cyclohexane-1,2,3-triol
DI109203
-
i.e. validamine
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
-
-
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
-
-
-
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
-
synthetic model compound
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
-
synthetic model compound
-
?
N-4-nitrophenyl-3-ketovalienamine
4-nitroaniline + ?
-
synthetic model compound
-
?
N-4-nitrophenyl-3-ketovalienamine
4-nitroaniline + ?
-
synthetic model compound
-
?
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
-
-
-
-
?
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
-
synthetic model compound
-
?
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
-
best substrate, C-O-lyase reaction
-
?
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
-
best substrate, C-O-lyase reaction
-
-
?
additional information
?
-
-
the enzyme has C-O-lyase activity
-
-
?
additional information
?
-
-
the enzyme has C-O-lyase activity
-
-
?
additional information
?
-
-
no substrates are O-4-nitrophenyl-beta-D-3-ketoglucoside, N-4-nitrophenylvalidamine, N-4-nitrophenyl-1-epi-3-ketovalidamine, O-4-nitrophenyl-alpha-D-glucoside
-
-
?
additional information
?
-
-
no substrates are O-4-nitrophenyl-beta-D-3-ketoglucoside, N-4-nitrophenylvalidamine, N-4-nitrophenyl-1-epi-3-ketovalidamine, O-4-nitrophenyl-alpha-D-glucoside
-
-
?
additional information
?
-
-
no substrates are N-4-nitrophenylvalienamine, O-4-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
no substrate is methyl-alpha-D-glucoside
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
positive cooperative interaction, maximal activation at 0.003 mM, kinetics
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4,6-Trinitrobenzenesulfonic acid
-
modification of amino group, 4-nitrophenyl-3-ketovalidamine protect, no protection by 4-nitrophenylvalidamine
diethyldicarbonate
-
modification of histidine residues, pH-dependent, hydroxylamine restores, substrates protect, no protection by 4-nitrophenyl-3-keto-1-epivalidamine, 4-nitrophenyl-beta-D-3-ketoglucoside, 4-nitrophenylvalidamine, 4-nitrophenyl-alpha-D-glucoside, methyl-alpha-D-glucoside, EGTA or CaCl2
EDTA
-
i.e. ethylenediamine tetra acetic acid, at 1 mM, 37°C, for 20 min., 100% inhibition, Ca2+ reverses, not Mg2+
additional information
-
at 1 mM, 37°C, for 20 min., no inhibited by p-chloromercuribenzoate and Mg2+, insignificant inhibition by Hg2+
-
EGTA
-
Ca2+ reverses; i.e. ethyleneglycol bis(beta-aminoethylether)-N,N'-tetraacetic acid, at 1 mM, 37°C, for 20 min., 100% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.006
2,4,6-Trinitrobenzenesulfonic acid
-
pH 9.5, 30°C, 10% glycerol, second order kinetics
0.23
diethyldicarbonate
-
pH 6.0, in ethanol, second order kinetics
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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
40
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pI VALUE
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
36000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
DI109203
putative N-terminal signal peptide, cleavage site is predicted between position 29 and 30
proteolytic modification
-
putative N-terminal signal peptide, cleavage site is predicted between position 29 and 30
-
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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
4°C, in 0.05 M phosphate buffer, pH 7, 60% loss of activity within 2 weeks, 2 weeks stable in the presence of 10% glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from soluble fraction, by ammonium sulfate fractionation, column chromatography on CM cellulose and gel filtration on Sephacryl S-200
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
3-ketovalidoxylamine C-N-lyase is one of three key enzymes in the production of valienamine, which is a potent glucosidase inhibitor from validamycin A. Increasing incidence of diabetes has focused attention on glucosidase inhibitors.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Asano, N.; Takeuchi, M.; Ninomiya, K.;Kameda, Y.; Matsui, K.
Microbial degradation of validamycin A by Flavobacterium saccharophilum. Enzymatic cleavage of C-N linkage in validoxylamine A
J. Antibiot.
37
859-867
1984
Flavobacterium saccharophilum
brenda
Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.
Purification and properties of 3-ketovalidoxylamine A C-N lyase from Flavobacterium saccharophilum
J. Biochem.
98
1631-1638
1985
Flavobacterium saccharophilum
brenda
Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.
Chemical modification by diethylpyrocarbonate of an essential histidine residue in 3-ketovalidoxylamine A C-N lyase
J. Biochem.
99
1571-1577
1986
Flavobacterium saccharophilum
brenda
Takeuchi, M.; Asano, N.; Kameda, Y.; Matsui, K.
Fluorometric studies on the role of calcium in substrate binding to 3-ketovalidoxylamine A C-N lyase
Chem. Pharm. Bull.
36
3540-3545
1988
Flavobacterium saccharophilum
brenda
Takeuchi, M.; Neyazaki, K.; Matsui, K.
Chemical modification by 2,4,6-trinitrobenzenesulfonic acid (TNBS) of an essential amino group in 3-ketovalidoxylamine A C-N lyase
Chem. Pharm. Bull.
38
1419-1420
1990
Flavobacterium saccharophilum
brenda
Zhang, J.F.; Zheng, Y.G.; Liu, Z.Q.; Shen, Y.C.
Preparation of 3-ketovalidoxylamine A C-N lyase substrate: N-p-nitrophenyl-3-ketovalidamine by Stenotrophomonas maltrophilia CCTCC M 204024
Appl. Microbiol. Biotechnol.
73
1275-1281
2007
Stenotrophomonas maltophilia
brenda
Zhang, J.; Zheng, Y.; Shen, Y.
Study on optimal production of 3-ketovalidoxylamine A C-N lyase and glucoside 3-dehydrogenase by a newly isolated Stenotrophomonas maltrophilia
Afr. J. Biotechnol.
8
5482-5488
2009
Stenotrophomonas maltophilia
-
brenda
Zhang, J.F.; Zheng, Y.G.; Shen, Y.C.
Purification and Characterization of 3-Ketovalidoxylamine A C-N Lyase Produced by Stenotrophomonas maltrophilia
Appl. Biochem. Biotechnol.
162
966-74
2010
Stenotrophomonas maltophilia
brenda
Kim, J.; Joo, J.; Kim, S.; Yoo, Y.
Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984
Biotechnol. Bioprocess Eng.
16
366-373
2011
Flavobacterium saccharophilum (DI109203), Flavobacterium saccharophilum IFO 13984 (DI109203)
-
brenda
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