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Information on EC 4.2.1.95 - kievitone hydratase
for references in articles please use BRENDA:EC4.2.1.95
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IUBMB Comments
The enzyme from Fusarium sp. hydrates the methylbutenyl sidechain of the isoflavonoid phytoalexins, thus reducing their toxicity.
The expected taxonomic range for this enzyme is: Fusarium solani species complex
showSynonyms
kievitone hydratase, nhkhs, khase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
hydratase, kievitone
-
-
-
-
KHase
-
-
-
-
NhKHS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
kievitone hydrate = kievitone + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
kievitone detoxification
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SYSTEMATIC NAME
IUBMB Comments
kievitone-hydrate hydro-lyase (kievitone-forming)
The enzyme from Fusarium sp. hydrates the methylbutenyl sidechain of the isoflavonoid phytoalexins, thus reducing their toxicity.
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CAS REGISTRY NUMBER
COMMENTARY
70431-10-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
8-prenylnaringenin + H2O
8-prenylnaringenin hydrate
Substrates: low activity
Products: -
Products: -
r
isoxanthohumol + H2O
isoxanthohumol hydrate
Substrates: -
Products: -
Products: -
r
xanthohumol
?
Substrates: XN, high activity with the recombinant enzyme
Products: -
Products: -
r
xanthohumol + H2O
xanthohumol hydrate
Substrates: XN, high activity with the recombinant enzyme
Products: -
Products: -
r
8-prenylnaringenin hydrate
8-prenylnaringenin + H2O
Substrates: -
Products: -
Products: -
r
8-prenylnaringenin hydrate
8-prenylnaringenin + H2O
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: -
Products: -
Products: -
r
isoxanthohumol hydrate
isoxanthohumol + H2O
Substrates: -
Products: -
Products: -
r
isoxanthohumol hydrate
isoxanthohumol + H2O
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: -
Products: -
Products: -
r
kievitone + H2O
kievitone hydrate
-
Substrates: -
Products: -
Products: -
?
kievitone + H2O
kievitone hydrate
Substrates: best substrate
Products: -
Products: -
r
kievitone + H2O
kievitone hydrate
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: best substrate
Products: -
Products: -
r
kievitone hydrate
kievitone + H2O
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: -
Products: -
Products: -
r
xanthohumol hydrate
xanthohumol + H2O
Substrates: -
Products: -
Products: -
r
xanthohumol hydrate
xanthohumol + H2O
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: the enzyme is a virulence factor, enzyme catalyses detoxification of a bean phytoalexin
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity analysis of the heterologously expressed recombinant enzyme, confirmation of HO-XN formation from XN by 1H-NMR and 13C-NMR in vitro
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme is a virulence factor, enzyme catalyses detoxification of a bean phytoalexin
Products: -
Products: -
?
kievitone hydrate
kievitone + H2O
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
Substrates: -
Products: -
Products: -
r
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
i.e. Fusarium solani subsp. pisi
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
-
brenda
additional information
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
-
brenda
additional information
-
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
-
brenda
additional information
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
-
brenda
additional information
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
-
brenda
additional information
-
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and serine 20. The signal peptide is absent from the predominantly secreted mature enzyme
-
brenda
additional information
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme contains a 19 amino acid-long N-terminal signal peptide whose cleavage site is predicted between alanine 19 and lysine 20. Absence of nucleotide cofactors is assumed due to the absence of a conserved nucleotide binding motif
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
the enzyme is a member of the hydrolyase enzyme group
evolution
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
evolution
the enzyme is a member of the hydrolyase enzyme group. Hydro-lyases are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
evolution
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme is a member of the hydrolyase enzyme group
-
evolution
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme belongs to the hydro-lyases, which are able to catalyze the highly selective, reversible addition of water to non-activated carbon-carbon double bonds and, thereby, generate primary, secondary or tertiary alcohols
-
physiological function
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
physiological function
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
kievitone hydratase catalyzes the addition of water to the double bond of the prenyl moiety of plant isoflavonoid kievitone and, thereby, forms the tertiary alcohol hydroxy-kievitone. In nature, this conversion is associated with a defense mechanism of fungal pathogens against phytoalexins generated by host plants after infection
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KHS_FUSSH
350
0
38970
Swiss-Prot
Chloroplast (Reliability: 5)
C7ZKN4_FUSV7
Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4)
348
0
38554
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
173000 - 175000
75000
recombinant His-tagged mature and glycosylated enzyme, gel filtration
97000 - 102000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
homodimer
2 * 48000, recombinant His-tagged mature and glycosylated enzyme, SDS-PAGE
homodimer
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
2 * 48000, recombinant His-tagged mature and glycosylated enzyme, SDS-PAGE
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
the enzyme contains four typical consensus sequences for N-linked glycosylation. The temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
glycoprotein
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
the enzyme contains four typical consensus sequences for N-linked glycosylation. The temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
additional information
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
additional information
-
the temperature stability of the enzyme is apparently not affected by deglycosylation in vivo, while in vitro activity assays show that the activity of the deglycosylated enzyme is approx. 30% lower compared to the glycosylated control
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
chloroform
DMSO
dodecane
Ethanol
hexane
additional information
chloroform
does affect the activity up to 5%, slight inhibition of xanthohumol hydrate formation at 10%, moderate inhibition at 30%
chloroform
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
does affect the activity up to 5%, slight inhibition of xanthohumol hydrate formation at 10%, moderate inhibition at 30%
-
DMSO
slight inhibition of xanthohumol hydrate formation at 5%, higher inhibition at 10%, complete inhibition at 30%
DMSO
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
slight inhibition of xanthohumol hydrate formation at 5%, higher inhibition at 10%, complete inhibition at 30%
-
dodecane
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
does affect the activity up to 30%
-
Ethanol
does affect the activity up to 5%, moderate inhibition of xanthohumol hydrate formation at 10%, strong inhibition at 30%
Ethanol
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
does affect the activity up to 5%, moderate inhibition of xanthohumol hydrate formation at 10%, strong inhibition at 30%
-
hexane
does affect the activity up to 25%, slight inhibition of xanthohumol hydrate formation at 30%
hexane
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
does affect the activity up to 25%, slight inhibition of xanthohumol hydrate formation at 30%
-
additional information
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
additional information
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
additional information
-
the polarity of the organic solvent is a determining factor for its effect on NhKHS activity, with increasing solubility in water resulting in a more distinct impact. This might be caused by an enhanced perturbing effect on the hydration shell of the enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His10-tagged enzyme from Pichia pastoris strain CBS7435 by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, higher functional recombinant expression of codon-harmonized gene encoding the enzyme in Pichia pastoris (i.e. Komagataella phaffii) strain CBS7435 as C-terminally His10-tagged protein, the mature enzyme is secreted. Upscaling tests show that Pichia pastoris is a most appropriate host for producing high amounts of recombinant NhKHS
DNA and amino acid sequence determination and analysis, sequence comparisons, lower functional recombinant expression of codon-harmonized gene encoding the enzyme in Pichia pastoris (i.e. Komagataella phaffii) strain CBS7435 as C-terminally His10-tagged protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds. The compatibility of enzyme NhKHS with nonpolar organic solvents is beneficial for a number of biocatalytic applications, e.g. in general for conversion of hydrophobic substrates
synthesis
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds
synthesis
Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
-
due to its catalytic properties and apparent substrate promiscuity, enzyme NhKHS is a promising enzyme for the biocatalytic production of tertiary alcohols. The production of enantiopure tertiary alcohols is a major challenge of organic synthesis as these functional groups are widely applicable for the generation of pharmaceuticals or other bioactive compounds. The compatibility of enzyme NhKHS with nonpolar organic solvents is beneficial for a number of biocatalytic applications, e.g. in general for conversion of hydrophobic substrates
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Turbek, C.S.; Smith, D.A.; Schardl, C.L.
An extracellular enzyme from Fusarium solani f. sp. phaseoli which catalyzes hydration of the isoflavonoid phytoalexin phaseolidin
FEMS Microbiol. Lett.
94
187-190
1992
Fusarium phaseoli
brenda
Turbek, C.S.; Li, D.; Choi, G.H.; Schardl, C.L.; Smith, D.A.
Induction and purification of kievitone hydratase from Fusarium solani f. sp. phaseoli
Phytochemistry
29
2841-2846
1990
Fusarium phaseoli
brenda
Cleveland, T.E.; Smith, D.A.
Partial purification, and further characterization, of kievitone hydratase from cel--free culture filtrates of Fusarium solani f. sp. phaseoli
Physiol. Plant Pathol.
22
129-142
1983
Fusarium phaseoli
-
brenda
Kuhn, P.J.; Smith, D.A.
Isolation from Fusarium solani f. sp. phaseoli of an enzymic system responsible for kievitone and phaseolidin detoxification
Physiol. Plant Pathol.
14
179-190
1979
Fusarium phaseoli
-
brenda
Li, D.; Chung, K.R.; Smidt, D.A.; Schardl, C.L.
The fusarin solani gene encoding kievitone hydratase, a secreted enzyme that catalyzes detoxification of a phytoalexin
Mol. Plant Microbe Interact.
8
388-397
1995
Fusarium phaseoli
brenda
Engleder, M.; Horvat, M.; Emmerstorfer-Augustin, A.; Wriessnegger, T.; Gabriel, S.; Strohmeier, G.; Weber, H.; Mueller, M.; Kaluzna, I.; Mink, D.; Schuermann, M.; Pichler, H.
Recombinant expression, purification and biochemical characterization of kievitone hydratase from Nectria haematococca
PLoS ONE
13
e0192653
2018
Fusarium solani (C7ZKN4), Fusarium solani (Q00870), Fusarium solani, Fusarium solani 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI (C7ZKN4)
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.95)
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