Information on EC 4.3.3.1 - 3-ketovalidoxylamine C-N-lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.3.3.1
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RECOMMENDED NAME
GeneOntology No.
3-ketovalidoxylamine C-N-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-nitrophenyl-3-ketovalidamine = 4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
show the reaction diagram
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
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-
-
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cleavage of C-O-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.
CAS REGISTRY NUMBER
COMMENTARY hide
99889-98-2
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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
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
show the reaction diagram
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
show the reaction diagram
4-nitrophenyl-3-keto-validamine
4-nitroaniline + ?
show the reaction diagram
-
assay at pH 7.0, 40C
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-
?
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + ?
show the reaction diagram
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assay at pH 7.0
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-
?
methyl-alpha-D-3-ketoglucoside + ?
?
show the reaction diagram
-
-
-
-
?
N-4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxy-2-cyclohexen-1-one
show the reaction diagram
N-4-nitrophenyl-3-ketovalienamine
4-nitroaniline + ?
show the reaction diagram
O-4-nitrophenyl-alpha-D-3-ketoglucoside
4-nitrophenol + 1,5-anhydro-D-erythro-hex-1-en-3-ulose
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
4-nitrophenyl-3-ketovalidamine
4-nitroaniline + 5-D-(5/6)-5-C-(hydroxymethyl)-2,6-dihydroxycyclohex-2-en-1-one
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2',2'',2'''-(1,2-ethanediyldinitrilo)tetraacetic acid
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2,4,6-Trinitrobenzenesulfonic acid
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modification of amino group, 4-nitrophenyl-3-ketovalidamine protect, no protection by 4-nitrophenylvalidamine
4-nitroaniline
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inhibition at low concentration
Co2+
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at 1 mM, 37.4% inhibition
Cu2+
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at 1 mM, 13.5% inhibition
diethyldicarbonate
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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
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i.e. ethylenediamine tetra acetic acid, at 1 mM, 37C, for 20 min., 100% inhibition, Ca2+ reverses, not Mg2+
La3+
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at 1 mM, 97.4% inhibition
Mn2+
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at 1 mM, 92.8% inhibition
Sr2+
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at 1 mM, 69.0% inhibition
additional information
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at 1 mM, 37C, for 20 min., no inhibited by p-chloromercuribenzoate and Mg2+, insignificant inhibition by Hg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
4-nitrophenyl-3-ketovalidamine
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0.24
N-4-nitrophenyl-3-ketovalidamine
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pH 8, 37C
2.5
N-4-Nitrophenyl-3-ketovalienamine
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pH 7, 37C
0.5
p-nitrophenyl-alpha-D-3-ketoglucoside
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pH 7, 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
2,4,6-Trinitrobenzenesulfonic acid
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pH 9.5, 30C, 10% glycerol, second order kinetics
0.23
diethyldicarbonate
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pH 6.0, in ethanol, second order kinetics
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.94
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after complete purification
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
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no activity below pH 5 and above pH 11
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
DI109203
x * 40878, calculated, x * 40000, SDS-PAGE
40878
DI109203
x * 40878, calculated, x * 40000, SDS-PAGE
additional information
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amino acid composition
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 36000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10.5
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701773
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme sensitive to heat
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 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
367.5fold by column chromatography
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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
expression in Escherichia coli
DI109203
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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.