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Information on EC 1.5.99.12 - cytokinin dehydrogenase
for references in articles please use BRENDA:EC1.5.99.12
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EC Tree 1 Oxidoreductases
1.5 Acting on the CH-NH group of donors
1.5.99 With unknown physiological acceptors
1.5.99.12 cytokinin dehydrogenase
IUBMB Comments
A flavoprotein (FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and copper(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.5.99.12
- trans-zeatin
- riboside
- cis-zeatin
-
isopentenyltransferase
-
cytokinin-deficient
- agriculture
Reaction Schemes
showN6-prenyladenine
+
+
=
+
+
Synonyms
cytokinin oxidase, cytokinin oxidase/dehydrogenase, cytokinin dehydrogenase, osckx2, hvckx1, zmckx1, zmcko1, atckx2, atckx7, atckx3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtCKX2
CKO
CKX
CKX1
CKX2
CKX3
CKX5
CKX6
CKX7
CKX8
CKX9
cytokinin oxidase
cytokinin oxidase/dehydrogenase
isopentenyladenosine oxidase
-
-
-
-
N6-(D2-isopentenyl)adenosine oxidase
-
-
-
-
N6-isopentenylaldenine oxidase
-
-
-
-
zeatin oxidase
-
-
-
-
additional information
AtCKX2
-
seven distinct genes AtCKX1 to AtCKX7, AtCKX2 is subject of the study
cytokinin oxidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
reaction scheme and mechanism, reduction of N6-(2-isopentenyl)adenine is rapidly performed, the reaction with O2 is slowly
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
reaction scheme and mechanism, the substrate displays a plug-into-socket binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin, bipartite architecture of the catalytic centre, which consists of a funnel-shaped region on the protein surface and an internal cavity lined by the flavin ring, the 3 active site regions are connected by a pore of about 4 A diameter
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
reaction might also be catalyzed by a different enzyme in Dictyostelium discoideum, since no related sequence has been found
-
N6-prenyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
Asp162 and Glu275 involved in substrate binding
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
N6-dimethylallyladenine:acceptor oxidoreductase
A flavoprotein (FAD). Catalyses the oxidation of cytokinins, a family of N6-substituted adenine derivatives that are plant hormones, where the substituent is a prenyl group. Although this activity was previously thought to be catalysed by a hydrogen-peroxide-forming oxidase, this enzyme does not require oxygen for activity and does not form hydrogen peroxide. 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, phenazine methosulfate and copper(II) in the presence of imidazole can act as acceptors. This enzyme plays a part in regulating rice-grain production, with lower levels of the enzyme resulting in enhanced grain production [2].
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CAS REGISTRY NUMBER
COMMENTARY
55326-39-1
-
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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
cis-zeatin + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
cis/trans-zeatin riboside + FAD + H2O
adenine + ? + FADH2
Substrates: -
Products: -
Products: -
ir
cytokinin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
? + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
Substrates: -
Products: -
Products: -
?
cytokinin riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
? + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
Substrates: -
Products: -
Products: -
?
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
isopentenyladenine 9-glucoside + 2,6-dichlorophenolindophenol
adenine 9-glucoside + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
isopentenyladenosine + 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
isopentenyladenosine monophosphate + 2,6-dichlorophenolindophenol
adenosine monophosphate + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
kinetin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
Substrates: -
Products: -
Products: -
?
kinetin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: low activity
Products: -
Products: -
?
kinetin + electron acceptor
2-furaldehyde + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
kinetin riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
Substrates: -
Products: -
Products: -
?
m-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very low activity
Products: -
Products: -
?
N-benzyladenine + electron acceptor
benzaldehyde + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-(2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 1,4-naphthoquinone
?
-
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 1,4-naphthoquinone
adenine + 3-methylbut-2-enal + reduced 1,4-naphthoquinone
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) radical + H2O
adenine + 3-methylbut-2-enal + ?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
adenine + 3-methylbut-2-enal + reduced 2,3-dimethoxy-5-methyl-1,4-benzoquinone
Substrates: i.e. coenzyme Q0
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine + 3-methylbut-2-enal + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
Substrates: 4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
N6-(2-isopentenyl)adenine + 4-nitrosoresorcinol-1-monomethyl ether + H2O
adenine + 3-methylbut-2-enal + reduced 4-nitrosoresorcinol-1-monomethyl ether
-
Substrates: 4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + acceptor + H2O
?
-
Substrates: preferred substrate of isozyme AtCKX4
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + caffeic acid
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + coenzyme Q1
adenine + 3-methylbut-2-enal + reduced coenzyme Q1
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + cytochrome c
adenine + 3-methylbut-2-enal + reduced cytochrome c
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + daphnoretin
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + duroquinone
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + electron acceptor
adenine + 3-methylbut-2-enal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
N6-(2-isopentenyl)adenine + hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one + H2O
adenine + 3-methylbut-2-enal + reduced hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
Substrates: CKX1 is able to use hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one as a poor electron acceptor at neutral pH levels, but not in acidic pH levels
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + o-coumaric acid
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + O2
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + O2
adenine + 3-methylbut-2-enal + H2O2
Substrates: oxidative degradation of cytokinins, slow reaction, low substrate specificity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + plantacyanine
adenine + 3-methylbut-2-enal + reduced plantacyanine
Substrates: electron acceptor from spinach
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + potassium ferricyanide
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + rosmarinic acid
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + scopoletin
adenine + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + spinach plantacyanine
adenine + 3-methylbut-2-enal + reduced spinach plantacyanine
Substrates: -
Products: -
Products: -
r
N6-(2-isopentenyl)adenine + vitamin K1
adenine + 3-methylbut-2-enal + reduced vitamin K1
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + vitamin K3
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + vitamin K3
adenine + 3-methylbut-2-enal + reduced vitamin K3
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-glucoside + 3',5'-dimethoxy-4'-hydroxyacetophenone + H2O
adenine 9-beta-D-glucoside + 3-methylbut-2-enal + ?
Substrates: i.e. iP9G, best substrate for isozyme AtCKX1 at pH 5.0, 3',5'-dimethoxy-4-hydroxyacetophenone is the best acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 2,3,5-triphenyl-tetrazolium chloride + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + 3',5'-dimethoxy-4'-hydroxyacetophenone + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + ferricyanide + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ferrocyanide
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + ferricytochrome c + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ferrocytochrome c
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + NAD+ + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + O2 + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside + oxidized 2,6-dichlorophenolindophenol + H2O
adenine 9-beta-D-riboside + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-beta-D-riboside 5'-phosphate + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
adenine 9-beta-D-riboside 5'-phosphate + 3-methylbut-2-enal + ?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-glucoside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-riboside-5'-monophosphate + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenose + 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenosine + 2,6-dichlorophenol indophenol
?
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenosine + FAD
adenosine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(4-hydroxy-2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 2,3-dimetoxy-5-methyl-1,4-benzoquinone + H2O
?
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: artificial electron acceptor
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 4-methylcatechol + H2O
adenine + 3-methylbut-2-enal + reduced 4-methylcatechol
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + acetosyringone + H2O
adenine + 3-methylbut-2-enal + reduced acetosyringone
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methyl-2-butenal + CuCl + Cl-
-
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + guaiacol + H2O
adenine + 3-methylbut-2-enal + reduced guaiacol
N6-(DELTA2-isopentenyl)adenine-9-beta-D-glucoside + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: artificial electron acceptor
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + 4-methylcatechol + H2O
adenosine + 3-methylbut-2-enal + reduced 4-methylcatechol
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + acetosyringone + H2O
adenosine + 3-methylbut-2-enal + reduced acetosyringone
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + guaiacol + H2O
adenosine + 3-methylbut-2-enal + reduced guaiacol
N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
Substrates: i.e. isopentenyladenine, reaction via an imine intermediate
Products: -
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?
N6-dimethylallyladenine + FAD + H2O2
adenine + 3-methylbut-2-enal + FADH2 + O2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
?
N6-dimethylallyladenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
Substrates: i.e. isopentenyladenosine
Products: -
Products: -
ir
N6-hexyladenine + electron acceptor
hexanal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyl-2-(2-hydroxyethylamino)-9-methyladenine + electron acceptor
3-methyl-2-butenal + 2-hydroxyethylamino-9-methyladenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyl-2-methylthioadenine + electron acceptor
3-methyl-2-butenal + 2-methylthioadenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
?
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methyl-2-butenal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + CuCl2
adenine + 3-methyl-2-butenal + reduced electron acceptor
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
N6-isopentenyladenine 9-beta-D-glucoside + oxidized 2,6-dichlorophenolindophenol
adenine 9-beta-D-glucoside + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine-9-beta-D-glucoside + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
?
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenosine + 2,6-dichlorophenolindophenol
3-methylbut-2-enal + adenosine + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
N6-isopentenyladenosine + oxidized 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-methyl-isopentenyladenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very low activity
Products: -
Products: -
?
O-beta-D-glucosyl-trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
Substrates: -
Products: -
Products: -
?
o-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very low activity
Products: -
Products: -
?
p-topolin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very low activity
Products: -
Products: -
?
trans-zeatin + 2,3-dimethoxy-5-methyl-1,4-benzoquinone + H2O
?
Substrates: -
Products: -
Products: -
?
trans-zeatin + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very effective substrate
Products: -
Products: -
?
trans-zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: cis-zeatin is utilized only by some tissue-specific forms but not by HvCKX2
Products: -
Products: -
?
trans-zeatin + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
trans-zeatin + electron acceptor
(2E)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
trans-zeatin 9-glucoside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: low activity
Products: -
Products: -
?
trans-zeatin 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: very effective substrate
Products: -
Products: -
?
trans-zeatin O-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
trans-zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
trans-zeatin riboside + 2,6-dichlorophenolindophenol + H2O
?
Substrates: most favorable substrate
Products: -
Products: -
?
trans-zeatin riboside O-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
trans-zeatin ribotide + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
trans-zeatin-9-glucoside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
zeatin + 2,6-dichlorophenolindophenol
4-hydroxy-3-methylbut-2-enal + adenine + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
zeatin + FAD + H2O
adenine + 4-hydroxy-3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
cis-zeatin + acceptor + H2O
?
-
Substrates: preferred substrate of isozyme ZmCKX10
Products: -
Products: -
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
cis-zeatin + electron acceptor
(2Z)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
Substrates: -
Products: -
Products: -
?
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
Substrates: -
Products: -
Products: -
?
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: -
Products: -
Products: -
ir
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
isopentenyladenosine + acceptor + H2O
? + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
isopentenyladenosine + acceptor + H2O
? + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
-
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
-
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
Substrates: very effective electron acceptor
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + CuCl2
?
-
Substrates: low activity
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
Substrates: the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: formation of a binary enzyme-product complex between the cytokinin imine and the reduced enzyme. The binary complex of the reduced enzyme and imine product intermediate decays relatively slowly to form an unbound product, cytokinin imine, which accumulates in the reaction mixture
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: -
Products: -
Products: -
?
N6-(2-isopentenyl)adenine 9-riboside + 2,3-dimethoxy-5-methyl-p-benzoquinone
?
-
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
Substrates: preferred substrate
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: oxidative degradation of cytokinins
Products: -
Products: -
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + guaiacol + H2O
adenine + 3-methylbut-2-enal + reduced guaiacol
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + guaiacol + H2O
adenine + 3-methylbut-2-enal + reduced guaiacol
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + guaiacol + H2O
adenosine + 3-methylbut-2-enal + reduced guaiacol
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + guaiacol + H2O
adenosine + 3-methylbut-2-enal + reduced guaiacol
Substrates: -
Products: -
Products: -
?
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
-
Substrates: -
Products: -
Products: -
ir
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
Substrates: substrate binding mechanism and structure, overview
Products: -
Products: -
ir
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: i.e. isopentenyladenine
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: FAD is cofactor
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: FAD is cofactor
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
Substrates: FAD is cofactor
Products: -
Products: -
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: oxidative degradation
Products: -
Products: -
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: substrate binding mechanism and structure, overview
Products: -
Products: -
ir
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
trans-zeatin + acceptor + H2O
?
-
Substrates: preferred substrate of isozymes AtCKX4 and AtCKX1
Products: -
Products: -
?
trans-zeatin + acceptor + H2O
?
-
Substrates: preferred substrate of isozymes ZmCKX1 and ZmCKX10
Products: -
Products: -
?
trans-zeatin + FAD + H2O
? + FADH2
Substrates: substrate binding mechanism and structure, overview
Products: -
Products: -
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: -
Products: -
Products: -
ir
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
Substrates: -
Products: -
Products: -
?
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
Substrates: -
Products: -
Products: -
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
Substrates: -
Products: -
Products: -
ir
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
Substrates: -
Products: -
Products: -
?
zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: -
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: -
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Phaseolus sp.
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: -
Products: -
Products: -
ir
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
Substrates: -
Products: -
Products: -
?
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
Substrates: the free bases and their ribosides are the preferred substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: the free bases and their ribosides are the preferred substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, by controlling the cytokinin level enzyme controls proliferation and differentiation of plant cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with dihydrozeatin
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with vitamin K1 as electron acceptor
Products: -
Products: -
?
additional information
?
-
-
Substrates: AtCKX2 prefers p-quinones and 2,6-dichlorophenol indophenol as electron acceptors, low reactivity with oxygen
Products: -
Products: -
?
additional information
?
-
-
Substrates: acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
Products: -
Products: -
?
additional information
?
-
Substrates: acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
Products: -
Products: -
?
additional information
?
-
Substrates: acceptor and substrate specificity, overview. The enzyme catalyzes the irreversible cleavage of N6-side chains from cytokinins. CKXs also show low cytokinin oxidase activity, but molecular oxygen is a comparatively poor electron acceptor. Vacuolar AtCKX enzymes in certain conditions degrade N6-(2-isopentenyl)adenine di- and triphosphates two to 5times more effectively than its monophosphate
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: analysis of enzyme activity regulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity, recombinant HvCKX2 prefers cytokinin ribosides as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: tissue and isozyme-specific substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity
Products: -
Products: -
?
additional information
?
-
Substrates: tissue and isozyme-specific substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression changes differently due to stress response in the 2 pea cultivars
Products: -
Products: -
?
additional information
?
-
-
Substrates: involvement of cytokinin oxidase/dehydrogenase in regulation of cytokinin levels in leaves
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, results suggest that CKX is responsible for the changes in endogenous cytokinin pool in gibberellic acid-treated plants and most probably this enzyme represents an important link in gibberellic acid/cytokinin cross talk
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: endogenous cytokinin levels after induction with N6-benzylaminopurine, overview, apoplastic enzyme degradation pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: cytokinins stimulate pigment formation and nitrogen fixation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: reduced expression of OsCKX2 causes cytokinin accumulation in inflorescence meristems and increases the number of reproductive organs, resulting in enhanced grain yield
Products: -
Products: -
?
additional information
?
-
Phaseolus sp.
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with zeatin, zeatin riboside, or N6-(2-hydroxybenzyl)adenine
Products: -
Products: -
?
additional information
?
-
-
Substrates: effects of exogenously applied auxins on cytokinin levels in seedlings, overview, exogenously applied cytokinins increase the glycosylation level of endogenous cytokinins, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes during infection, cytokinins are involved in pathogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a major role in control of cytokinin plant hormone levels
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a major role in control of cytokinin plant hormone levels
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity with cytokinins, overiew
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity with cytokinins, overiew
Products: -
Products: -
?
additional information
?
-
Substrates: the substrate binding site is located at amino acid residues 245-491
Products: -
Products: -
?
additional information
?
-
-
Substrates: the substrate binding site is located at amino acid residues 245-491
Products: -
Products: -
?
additional information
?
-
Substrates: specificity for electron acceptors, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity for electron acceptors, overview
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: laccase and peroxidase catalyze oxidative cleavage of hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one (DIMBOA) to 4-nitrosoresorcinol-1-monomethyl ether (coniferron) which serves as a weak electron acceptor of CKX1. The oxidation of DIMBOA and coniferron generates transitional free radicals that are used by CKX1 as effective electron acceptors. hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-glucoside is not active as an electron acceptor for isozyme CKX1
Products: -
Products: -
?
additional information
?
-
Substrates: adenosine, abscisic acid, gibberellic acid, and cis-zeatin riboside are no substrates, nor is the reduced dihydrozeatin. Aromatic cytokinins, kinetin and N6-benzyladenine, and the synthetic substituted urea cytokinin thidiazuron are also inactive, as are most cytokinin glucosides and the monophosphate N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: adenosine, abscisic acid, gibberellic acid, and cis-zeatin riboside are no substrates, nor is the reduced dihydrozeatin. Aromatic cytokinins, kinetin and N6-benzyladenine, and the synthetic substituted urea cytokinin thidiazuron are also inactive, as are most cytokinin glucosides and the monophosphate N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
Substrates: the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
Products: -
Products: -
?
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
Substrates: -
Products: -
Products: -
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: oxidative degradation
Products: -
Products: -
ir
trans-zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + electron acceptor
4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
Substrates: -
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + 4-hydroxy-3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: oxidative degradation of cytokinins
Products: -
Products: -
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: -
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Phaseolus sp.
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
Substrates: -
Products: -
Products: -
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: -
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
Phaseolus sp.
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
zeatin + FAD + H2O
adenine + ? + FADH2
-
Substrates: enzyme catalyzes the irreversible degradation of cytokinins
Products: -
Products: -
ir
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, by controlling the cytokinin level enzyme controls proliferation and differentiation of plant cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
Substrates: analysis of enzyme activity regulation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression changes differently due to stress response in the 2 pea cultivars
Products: -
Products: -
?
additional information
?
-
-
Substrates: involvement of cytokinin oxidase/dehydrogenase in regulation of cytokinin levels in leaves
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, results suggest that CKX is responsible for the changes in endogenous cytokinin pool in gibberellic acid-treated plants and most probably this enzyme represents an important link in gibberellic acid/cytokinin cross talk
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: endogenous cytokinin levels after induction with N6-benzylaminopurine, overview, apoplastic enzyme degradation pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: cytokinins stimulate pigment formation and nitrogen fixation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: reduced expression of OsCKX2 causes cytokinin accumulation in inflorescence meristems and increases the number of reproductive organs, resulting in enhanced grain yield
Products: -
Products: -
?
additional information
?
-
Phaseolus sp.
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde
Products: -
Products: -
?
additional information
?
-
-
Substrates: effects of exogenously applied auxins on cytokinin levels in seedlings, overview, exogenously applied cytokinins increase the glycosylation level of endogenous cytokinins, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes during infection, cytokinins are involved in pathogenesis
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a major role in control of cytokinin plant hormone levels
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a major role in control of cytokinin plant hormone levels
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
Products: -
Products: -
?
additional information
?
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
Products: -
Products: -
?
additional information
?
-
-
Substrates: irreversible oxidative cleavage of the N6-side chain of cytokinins, products are adenine and side-chain derived aldehyde, important for the regulation of early development of the plant embryo
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,6-dichlorophenolindophenol
-
in vitro 4000fold faster reaction than with the native acceptor
FAD
binding site comprising amino acid residues 69-105, covalent binding through a histidine residue
additional information
enzyme shows a preference for quinones as electron acceptors
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24-epibrassinolide
-
inhibits both cytokinin oxidase activity and expression. Treatment with 0.4 mM 24-epibrassinolide leads to elevated cytokinin levels in roots and shoots, that are maintained only in the presence of 24-epibrassinolide, while the hormone removal leads to return of cytokinin concentration to the control level initially in the roots and then in the shoots
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
one of the most potent inhibitors of CKO
N-(2-amino-pyridin-4-yl)-N'-phenylurea
one of the most potent inhibitors of CKO
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
the compound binds in a planar conformation and competes for the same binding site with natural substrates
N6-(3-hydroxy-2-phenylethyl)-2-(3-hydroxypropylamino)-9-isopentenyladenine
-
-
N6-but-2,3-dienyl-aminopurine
-
mechanism-based irreversible (suicide) inhibitor. IC50: 0.02 mM with N6-(2-isopentenyl)adenine as substrate, 0.0004 mM with N6-(2-isopentenyl)adenosine as substrate and less than 0.0001 mM with zeatin as substrate
N6-pent-2,3-dienyl aminopurine
-
10%, 52%, and 86% inhibition at concentrations of 0.001 mM, 0.01 mM and 0.1 mM
additional information
cultivation in the presence of gibberillic acid reduces enzyme activity in leaves of cv. Manuela
-
additional information
enzyme is strongly inhibited by flavin-protein oxidoreductase inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
auxin treatment induces AtCKX6 gene and increases enzyme level
-
additional information
expression of the DhCKX gene is induced in roots, shoot apices and leaves, but not in stems, after treatment with 0.02 mM 6-benzylamino-purine
-
additional information
-
expression of the DhCKX gene is induced in roots, shoot apices and leaves, but not in stems, after treatment with 0.02 mM 6-benzylamino-purine
-
additional information
-
dark-treatment results in high increase in CKX activity, addition of kinetin in dark-treated leaves results in high increase of CKX activity compared with dark-treated leaves without kinetin
-
additional information
-
elevated temperature around 35°C increases enzyme activity
-
additional information
cultivation in the presence of gibberillic acid increases enzyme activity in leaves of cv. Scinado
-
additional information
-
cytokinin-induced up-regulation of enzyme activity, e.g. by N6-benzylaminopurine application on the plant leaf or callus surface leads to about 2.5fold increased activity after 4 h, overview
-
additional information
-
cytokinins induce enzyme activity, predominantly of the glycosylated isozyme
-
additional information
isozymes TaCKX5a/b, TaCKX6a, and TaCKX2a expression are induced by pathogen infection, i.e. by Fusarium sp. or Puccinia sp.
-
additional information
-
isozymes TaCKX5a/b, TaCKX6a, and TaCKX2a expression are induced by pathogen infection, i.e. by Fusarium sp. or Puccinia sp.
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Cytokinin oxidase activity and cytokinin content in roots of sunflower under water stress.
Dehydration
Cytokinin oxidase PpCKX1 plays regulatory roles in development and enhances dehydration and salt tolerance in Physcomitrella patens.
Infections
Combinatorially selected defense peptides protect plant roots from pathogen infection.
Infections
Stabilization of cytokinin levels enhances Arabidopsis resistance against Verticillium longisporum.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) radical
-
pH 5.0, temperature not specified in the publication
0.0041
4-nitrosoresorcinol-1-monomethyl ether
-
pH 5.0, in the presence of peroxidase, temperature not specified in the publication
0.0062
4-nitrosoresorcinol-1-monomethyl ether
-
pH 5.0, in the presence of laccase, temperature not specified in the publication
0.0113
4-nitrosoresorcinol-1-monomethyl ether
-
pH 7.0, in the presence of peroxidase, temperature not specified in the publication
0.192
4-nitrosoresorcinol-1-monomethyl ether
-
pH 5.0, temperature not specified in the publication
0.0089
hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
pH 5.0, in the presence of peroxidase, temperature not specified in the publication
0.0109
hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
pH 5.0, in the presence of laccase, temperature not specified in the publication
0.0345
hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
pH 7.0, in the presence of laccase, temperature not specified in the publication
0.113
hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
pH 7.0, in the presence of peroxidase, temperature not specified in the publication
0.25
hydroxamic acid 2,4-dihydroxy-7-methoxy-1,4-benzoxazin-one
-
Km above 0.25 mM, pH 7.0, temperature not specified in the publication
0.0011
N6-(2-isopentenyl)adenine
wild type enzyme, pH and temperature not specified in the publication
0.0015
N6-(2-isopentenyl)adenine
-
with 2,3-dimethoxy-5-methyl-p-benzoquinone, pH 7.0, 37°C
0.003
N6-(2-isopentenyl)adenine
mutant enzyme E381A, pH and temperature not specified in the publication
0.0032
N6-(2-isopentenyl)adenine
mutant enzyme E381S, pH and temperature not specified in the publication
0.001
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell culture medium induced by tetracycline, pH 6.0, 37°C
0.0015
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell extract induced by tetracycline, pH 6.0, 37°C
0.0017
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell culture medium induced by N6-benzylaminopurine, pH 6.0, 37°C
0.0022
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell extract, pH 6.0, 37°C
0.0023
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell extract induced by N6-benzylaminopurine, pH 6.0, 37°C
0.0025
N6-(DELTA2-isopentenyl)adenine
-
transgenic plant cells conditionally overexpressing isopentenyltransferase, cell culture medium, pH 6.0, 37°C
additional information
additional information
-
enzyme activity dynamics in relation to glycosylation level
-
additional information
additional information
kinetics, redox potential of electron acceptors
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
129.8
N6-(2-isopentenyl)adenosine
pH 6.5, recombinant enzyme, with cofactor 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5.4
N6-(2-isopentenyl)adenine
-
with 2,3-dimethoxy-5-methyl-p-benzoquinone, pH 7.0, 37°C
143.6
N6-(2-isopentenyl)adenine
pH 6.5, recombinant enzyme, with cofactor 2,3-dimethoxy-5-methyl-1,4-benzoquinone
additional information
additional information
at pH above pH 6.5 polymerization of the quinone acceptors occur
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02 - 2
N6-but-2,3-dienyl-aminopurine
Solanum tuberosum
-
mechanism-based irreversible (suicide) inhibitor. IC50: 0.02 mM with N6-(2-isopentenyl)adenine as substrate, 0.0004 mM with N6-(2-isopentenyl)adenosine as substrate and less than 0.0001 mM with zeatin as substrate
additional information
additional information
Arabidopsis thaliana
-
IC50-values above 0.1 mM for 2-chloro-6-(2-hydroxyanilino)purine, 2-chloro-6-(4-hydroxyanilino)purine, 2-chloro-6-(2-methoxyanilino)purine, 2-chloro-6-(4-methoxyanilino)purine, 2-methylthio-6-(3-methoxyanilino)purine and 2-chloro-6-(3-methoxyanilino)-9-isopropylpurine, no inhibition observed for 6-anilinopurine and trans-zeatin
-
0.004
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.007
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.007
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.009
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0002
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.006
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.006
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.039
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.017
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.13
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0001
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0004
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.001
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.006
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.017
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.05
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.002
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.003
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.004
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.009
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.008
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.02
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.00008
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0004
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0005
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.0045
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0011
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0015
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.006
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.022
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.024
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.032
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.00004
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.0006
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.0007
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.0018
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.00004
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.002
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.032
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.035
N-(2-amino-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.006
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.015
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.02
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.022
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.0015
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.003
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
0.004
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
0.018
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.035
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme L492A, pH and temperature not specified in the publication
0.042
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
wild type enzyme, pH and temperature not specified in the publication
0.045
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381A, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0003
0.0004
-
transgenic plant conditionally overexpressing isopentenyltransferase, cell extract, not induced cells
0.002
-
wild-type plant and transgenic plant conditionally overexpressing isopentenyltransferase, cell extract, N6-benzylaminopurine-induced
0.004
-
transgenic plant conditionally overexpressing isopentenyltransferase, cell culture medium of N6-benzylaminopurine-induced cells
0.005
-
wild-type plant, cell culture medium of N6-benzylaminopurine-induced cells
0.0052
-
N6-(2-isopentenyl)adenine + 2,3-dimethoxy-5-methyl-p-benzoquinone, pH 7.0, 37°C
0.0065
-
transgenic plant conditionally overexpressing isopentenyltransferase, cell culture medium of tetracycline-treated cells
additional information
0.0003
-
wild-type plant, cell extract and cell culture medium, not induced or tetracycline-treated cells
0.0003
-
transgenic plant conditionally overexpressing isopentenyltransferase, cell culture medium, not induced
additional information
-
specific activities given for all possible reactant pairs
additional information
-
specific activity in roots and leaves at different UV-B irradiation and temperatures levels, overview
additional information
-
assay development and optimization with 2,6-dichlorophenolindophenol as electron acceptor
additional information
activity in diverse tissues at pH 6.0 and pH 8.0, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
6.5
6.8
7 - 7.5
7.2
7.5
8.5
additional information
4.5
recombinant HvCKX2 expressed in tobacco, native overall enzyme activity in grains and leaves shows 2 maxima at pH 4.5 and at pH 7.0-7.5
4.5
native overall enzyme activity in grains and leaves shows 2 maxima at pH 4.5 and at pH 7.0-7.5
7 - 7.5
native overall enzyme activity in grains and leaves shows 2 maxima at pH 4.5 and at pH 7.0-7.5
additional information
Phaseolus sp.
-
the 2 isozymes show largely different different pH-optima
additional information
activity in diverse tissues at pH 6.0 and pH 8.0, overview
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
pH 6.0: about 45% of maximal activity, pH 10.0: aout 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
isoform CKX1, calculated from sequence
5.7
calculated from sequence
6.5
calculated from sequence
6.6
6.7
calculated from sequence
8.2
calculated from sequence
8.4
calculated from sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phytopathogen causing the witches broom disease, gene FasV of RfCKX1
-
-
brenda
cultivars Golden Promise, Scarlett, Torka, and Kontesa
SwissProt
brenda
cv. Luxor, gene HvCKX1, barley contains at least 7 different gene homologues
SwissProt
brenda
cv. Luxor, gene HvCKX2, barley contains at least 7 different gene homologues
SwissProt
brenda
cv. Luxor, gene HvCKX3, barley contains at least 7 different gene homologues
SwissProt
brenda
cv. Luxor, gene HvCKX7, genomic DNA, barley contains at least 7 different gene homologues, gene HvCKX7, genomic DNA
-
-
brenda
L. cv. Scinado and cv. Manuela, cv. Scinado normally requires shorter growing period than cv. Manuela
UniProt
brenda
PsCKX1; L. cv. Sparkle, wild type and R50 carrying a recessive sym16 which is a pleiotropic mutant of pea which develops few, pale nodules and has pale young leaves, R50 has reduced CKX activity and increased cytokinin level compared with wild type, sequencing of DNA from both strains did not show any obvious mutations within the gene
UniProt
brenda
cv. Wisconsin 38, wild-type, and transgenic tobacco conditionally overexpressing isopentenyltransferase IPT
-
-
brenda
Hedw., wild type and transgenic cells expressing the AtCKX2 gene from Arabidopsis thaliana, expression of AtCKX2 results in a significant decrease of cytokinin level and morphological changes such as altered morphology of filaments, impaired budding, and loss of sexual reproductivity
-
-
brenda
cv. Samantha, gene TaCKX1, wheat contains at least 8 different gene homologues
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the vascular tissue and medullary region of sepals and petals show slight activity of CKX
brenda
at early flowering: TaCKX7b and TaCKX8, at late flowering: TaCKX4
brenda
-
in the stalk of the leaf branched glandular trichomes, the CKX activity is restricted to the stalk region only, and is not present in the secretory head
brenda
additional information
-
first foliage leaves are cut of and kept in water in the darkness which results in a high increase in CKX activity
brenda
-
involvement of cytokinin oxidase/dehydrogenase in regulation of cytokinin levels in leaves
brenda
lower CK content and higher enzymatic activity in cv. Manuela leaves compared with cv. Scinado
brenda
-
diurnal variation. Maximal activity 3 h after the dark-light transition and during the diminishing of the midday cytokinin peak
brenda
Rhipsalidopsis sp.
-
greenhouse-grown, enzyme activity increases during subculturing
brenda
Schlumbergera sp.
-
greenhouse-grown, enzyme activity increases during subculturing
brenda
-
35 kDa isozyme CKX35 in chlorotic leaves associated with a reduction in representative cytokinin levels and high H2O2 concentrations, and 37 kDa isozyme CKX37 in green leaves associated with representative CKs and H2O2 at normal levels
brenda
-
35 kDa isozyme CKX35 in chlorotic leaves associated with a reduction in representative cytokinin levels and high H2O2 concentrations, and 37 kDa isozyme CKX37 in green leaves associated with representative CKs and H2O2 at normal levels
-
brenda
cv. Manuela has a higher endogenous cytokinin content and slightly lower enzyme activity than cv. Scinado
brenda
highest activity in root nodule, very low enzyme level in R50 mutant compared with wild type
brenda
-
after removal of roots, no cytokinin oxidase activity remains after 24 h
brenda
-
after removal of roots, no cytokinin oxidase activity remains after 24 h
-
brenda
additional information
-
isozyme AtCKX1 is expressed in all plant organs
brenda
additional information
-
tissue specific and developmental expression of barley isozymes, overview
brenda
additional information
tissue specific and developmental expression of barley isozymes, overview
brenda
additional information
tissue specific and developmental expression of barley isozymes, overview
brenda
additional information
tissue specific and developmental expression of barley isozymes, overview
brenda
additional information
-
enzyme activity during vegetative development of plants
brenda
additional information
tissue specific expression of wheat isozymes
brenda
additional information
-
tissue specific expression of wheat isozymes
brenda
additional information
-
the enzyme activity is not detected in the epidermal layers of leaf, stem and root, but the epidermal outgrowth and the leaf trichome show prominent CKX activity
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
secretion pathway, enzymes AtCKX2, and AtCKX3-AtCKX6
-
brenda
-
secretion pathway, the glycosylated isozyme accumulates preferentially in the culture medium
-
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
malfunction
metabolism
physiological function
evolution
the CKX gene family of Arabidopsis thaliana comprises seven members
evolution
a total of 8 cytokinin dehydrogenase CKX gene family members are identified from 'Kyoho' grape genome. All CKXs have 3-5 introns. The CKX family members have two highly conserved domains: an oxidase FAD-binding domain and a cytokinin dehydrogenase 1, FAD/cytokinin binding domain
evolution
-
in 228 barley landraces and 216 wild accessions, 14 haplotypes of gene CKX2 have been identified, five of these with ten or more members, coding for four different protein variants. The amino acid substitution specific to haplotype 3 can result in a change in the functional properties of the CKX2 protein. Haplotypes 1-3 have overlapping geographical distributions in the wild population, but the average rainfall amounts at the collection sites for haplotype 3 plants are significantly higher during November to February compared to the equivalent data for plants of haplotypes 1 and 2
malfunction
silencing of the CKX1 gene decreases the cytokinin oxidase/dehydrogenase level in barley and leads to higher plant productivity (number of seeds per plant) and root weight
malfunction
-
silencing of the CKX1 gene decreases the cytokinin oxidase/dehydrogenase level in barley and leads to higher plant productivity (number of seeds per plant) and root weight
malfunction
-
inhibition of the enzyme by 24-epibrassinolide leads to activation of production of cytokinins in roots and shoots, of which excessive amounts are transferred into the storage forms
malfunction
-
overexpression of the AtCKX genes in tobacco leads to shoot senescence, an increase of the root meristem zone, and enhanced formation of lateral roots
malfunction
-
silencing of the HvCKX1 gene of barley cytokinin oxidase leads to a significant inhibition of cytokinin oxidase activity accompanied by an increase in productivity of this culture
malfunction
-
chlorotic leaves associated with a reduction in representative Ccytokinin levels and high H2O2 concentrations under drought, salt and iron-deficiency stresses of tomato plants.Chlorosis-inducing stresses (salt and iron-deficiency) induce lower chlorophyll levels as compared to drought stress and control, overview
malfunction
-
inhibition of the enzyme by 24-epibrassinolide leads to activation of production of cytokinins in roots and shoots, of which excessive amounts are transferred into the storage forms
-
malfunction
-
chlorotic leaves associated with a reduction in representative Ccytokinin levels and high H2O2 concentrations under drought, salt and iron-deficiency stresses of tomato plants.Chlorosis-inducing stresses (salt and iron-deficiency) induce lower chlorophyll levels as compared to drought stress and control, overview
-
metabolism
-
comparison of the functional spectra of cytokinins and brassinosteroids, overview
metabolism
-
comparison of the functional spectra of cytokinins and brassinosteroids, overview
-
physiological function
cytokinin oxidase/dehydrogenase irreversibly degrades the plant hormones cytokinins and thereby participates in their homeostasis
physiological function
-
cytokinin oxidase is involved in the regulation of cytokinin content by 24-epibrassinolide in wheat seedlings
physiological function
-
cytokinins are plant growth regulators playing crucial role in almost all the developmental processes. Oxidative breakdown of cytokinins by cytokinin oxidase is an important process by which plant tissues control the levels and distribution of cytokinins
physiological function
cytokinin oxidase/dehydrogenase plays an important role in regulating plant growth and development
physiological function
-
the regulation of CKO activity might be one of the important mechanisms determining plant response to treatments via the changes in the cytokinin concentration. The presence of apoplastic (xylem) cytokinins located outside the cells may be important because the receptors of cytokinins initiating activation of CKO gene expression are located in the cell membrane
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
the enzyme catalyzes the irreversible degradation of cytokinin phytohormones that are extremely necessary for growth, development, and differentiation of plants. Cytokinin oxidase plays an important role in the regulation of levels of cytokinin hormones, the enzyme directly influences cytokinin-regulated physiological processes in plants
physiological function
-
cytokinin dehydrogenase catalyzes the irreversible degradation of cytokinins, that play a role in the regulation of hydrogen peroxide accumulation while H2O2 is involved in chlorophyll degradation. CKX differentially regulates representative cytokinin levels and indirectly influence H2O2 accumulation in tomato leaves.mechanism, overview. The CKX isoforms in the tomato leaf appear to have distinct roles in differentially regulating CK levels and indirectly influencing H2O2 accumulation
physiological function
transgenic barley overexpressing the cytokinin dehydrogenase gene CKX1 shows greater tolerance to drought stress
physiological function
isoform CKX1 is a key regulator of active cytokinin levels in developing maize roots
physiological function
a CKX2 mutant shows longer panicle with dense branching pattern and higher seed setting rate compared to the wild-type. The grains in the mutant are markedly longer, wider, and heavier compared to the wild-type. A higher number of the spikelet cells with bigger size result in larger grains in the mutant strain. Mutant panicles have a decreased CKX2 expression in and display reduced cytokinin dehydrogenase enzyme activity, leading to remarkably higher endogenous cytokinin content
physiological function
-
cytokinin oxidase is involved in the regulation of cytokinin content by 24-epibrassinolide in wheat seedlings
-
physiological function
-
cytokinin oxidase/dehydrogenase plays an important role in regulating plant growth and development
-
physiological function
-
the regulation of CKO activity might be one of the important mechanisms determining plant response to treatments via the changes in the cytokinin concentration. The presence of apoplastic (xylem) cytokinins located outside the cells may be important because the receptors of cytokinins initiating activation of CKO gene expression are located in the cell membrane
-
physiological function
-
cytokinin dehydrogenase catalyzes the irreversible degradation of cytokinins, that play a role in the regulation of hydrogen peroxide accumulation while H2O2 is involved in chlorophyll degradation. CKX differentially regulates representative cytokinin levels and indirectly influence H2O2 accumulation in tomato leaves.mechanism, overview. The CKX isoforms in the tomato leaf appear to have distinct roles in differentially regulating CK levels and indirectly influencing H2O2 accumulation
-
Show AA Sequence and Transmembrane Helices (4036 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53300
-
x * 61000, SDS-PAGE, weak bands also at 75000 Da and100000 Da, x * 53300, calculated from the deduced amino acid sequence
56000
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
56500
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
57400
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
57900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
58000
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
58080
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
58100
58400
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
58800
59100
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
59400
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
59720
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
59900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
60000
60383
x * 60383, calculated from the deduced amino acid sequence
61000
-
x * 61000, SDS-PAGE, weak bands also at 75000 Da and100000 Da, x * 53300, calculated from the deduced amino acid sequence
64290
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
64900
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
65050
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
92000
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
97000
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
58100
x * 58100, HvCKX3, amino acid sequence calculation
58100
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
58800
x * 58800, HvCKX2, amino acid sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
x * 61000, SDS-PAGE, weak bands also at 75000 Da and100000 Da, x * 53300, calculated from the deduced amino acid sequence
?
x * 64900, AtCKX1, amino acid sequence calculation, x * 57400, AtCKX2, amino acid sequence calculation, x * 59400, AtCKX3, amino acid sequence calculation, x * 58100, AtCKX4, amino acid sequence calculation, x * 59900, AtCKX5, amino acid sequence calculation, x * 56500, AtCKX6, amino acid sequence calculation, x * 57900, AtCKX7, amino acid sequence calculation
?
x * 97000, SDS-PAGE, x * 65050, sequence calculation, x * 64290, mass spectrometry
?
x * 92000, SDS-PAGE, x * 59720, sequence calculation, x * 58080, mass spectrometry
?
-
x * 59100, OsCKX1, amino acid sequence calculation, x * 56000, OsCKX2, amino acid sequence calculation, x * 58000, OsCKX3and OsCKX5, amino acid sequence calculation, x * 58400, OsCKX4, amino acid sequence calculation
?
x * 46600, calculated from sequence
?
x * 57140, calculated from sequence
?
x * 58690, calculated from sequence
?
x * 70340, calculated from sequence
?
x * 58150, calculated from sequence
?
x * 62880, calculated from sequence
?
x * 58520, calculated from sequence
?
x * 61920, calculated from sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no glycoprotein
glycoprotein
enzyme amino acid sequences encoded by the 7 distinct genes in Arabidopsis contain 3 to 8 putative glycosylation sites, overview
glycoprotein
-
three N-glycosylation sites, glycosylation of the enzyme can explain the difference between theoretical and experimental weight
glycoprotein
enzyme amino acid sequence contains 2 putative glycosylation sites
glycoprotein
enzyme amino acid sequence contains 5 putative glycosylation sites
glycoprotein
enzyme amino acid sequence contains 5 potential glycosylation sites
glycoprotein
-
high increase in enzyme glycosylation rate during dark-treatment
glycoprotein
-
enzyme binds with moderate affinity to concanavalin A, glycosylation is influenced by cytokinins and has a regulatory role for the enzyme activity, glycosylation changes the enzyme secretion level
glycoprotein
-
enzyme amino acid sequences encoded by the 5 distinct genes in rice contain 1-6 putative glycosylation sites
glycoprotein
-
enzyme amino acid sequence contains 2 putative glycosylation sites
glycoprotein
enzyme amino acid sequence contains 5-8 putative glycosylation sites
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method in the presence of N6-(buta-2,3-dienyl)adenine or N6-(penta-2,3-dienyl)adenine
purified free recombinant enzyme, or purified recombinant enzyme complexed with trans-zeatin, N6-isopentenyladenine, and N6-benzyladenine, sitting drop vapour diffusion method, 20°C, protein solution: 30 mg/ml protein, 20 mM HEPES-KOH, pH 7.5, mixed with equal volume of well solution containing 0.1 M sodium acetat, pH 4.6, 0.2 M ammonium sulfate, and 12% w/v PEG 5000 monomethylether, a few hours, soaking in ligand solution and/or cryoprotectant 30% glycerol before data collection, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution, single isomorphous replacement, Fourier methods
purified recombinant enzyme, 20 mg/ml protein with 0.5% w/v n-octyl-beta-D-glucopyranoside, hanging drop vapour diffusion method, 0.002 ml protein solution mixed with 0.002 ml reservoir solution containing 30% w/v PEG 1500, 0.1 M Tris-HCl, pH 7.0, 1 week, 20°C, X-ray diffraction structure determination and analysis at 1.95 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E381A
the mutation mimics the active site composition of naturally occurring isozymes CKO4/6 and CKO2/3
E381S
the mutation mimics the active site composition of naturally occurring isozymes CKO4/6 and CKO2/3
L492A
the mutant retains an unchanged pattern of selectivity to variously substituted ureas but it is much more susceptible to the inhibition by phenylureas as IC50 values are 10-50times lower than those for wild type enzyme
additional information
additional information
transgenic tobacco plants overexpressing ArCKX1, AtCKX5, or AtCKX6 shows increased enzyme activity and reduced cytokinin content phenotype, phenotypic effects of enzyme overexpression in transgenic Arabidopsis plants, overview
additional information
-
transgenic tobacco plants overexpressing ArCKX1, AtCKX5, or AtCKX6 shows increased enzyme activity and reduced cytokinin content phenotype, phenotypic effects of enzyme overexpression in transgenic Arabidopsis plants, overview
additional information
-
overexpression of the AtCKX genes in tobacco leading to shoot senescence, an increase of the root meristem zone, and enhanced formation of lateral roots
additional information
-
transgenic tobacco plants overexpressing HvCKX2 show a very strong phenotype of cytokinin deficiency with shorter interndes, highly increased formation of roots, and a dwarf growth habit, and died without producing seeds
additional information
transgenic tobacco plants overexpressing HvCKX2 show a very strong phenotype of cytokinin deficiency with shorter interndes, highly increased formation of roots, and a dwarf growth habit, and died without producing seeds
additional information
transgenic tobacco plants overexpressing HvCKX2 show a very strong phenotype of cytokinin deficiency with shorter interndes, highly increased formation of roots, and a dwarf growth habit, and died without producing seeds
additional information
transgenic tobacco plants overexpressing HvCKX2 show a very strong phenotype of cytokinin deficiency with shorter interndes, highly increased formation of roots, and a dwarf growth habit, and died without producing seeds
additional information
-
overexpression of HvCKX3 in transgenic tobacco plants does not lead to increased enzyme activity or an altered phenotype
additional information
overexpression of HvCKX3 in transgenic tobacco plants does not lead to increased enzyme activity or an altered phenotype
additional information
overexpression of HvCKX3 in transgenic tobacco plants does not lead to increased enzyme activity or an altered phenotype
additional information
overexpression of HvCKX3 in transgenic tobacco plants does not lead to increased enzyme activity or an altered phenotype
additional information
-
construction of transgenic tobacco plants conditionally overexpressing isopentenyltransferase IPT, tetracycline-induced derepressing of the IPT transcription, results in enhanced cytokinin oxidase activity
additional information
-
phenotypic effects of enzyme overexpression in transgenic tobacco, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation
recombinant from yeast Yarrowia lipolytica by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
recombinant vacuolar His-tagged isozyme AtCKX1 41.7fold from Pichia pastoris by ultrafiltration, hydrophobic interaction and hydroxyapatite chromatography, followed by nickel affinity chromatography and another step of hydrophobic interaction chromatography
recombinant vacuolar isozyme AtCKX3 18fold from Pichia pastoris by ultrafiltration, hydroxyapatite chromatography, nickel affinity chromatography, and anion exchange chromatography and another step of hydrophobic interaction chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
5 distinct genes OsCKX1-OsCKX5, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
7 distinct genes, AtCKX1-AtCKX7, DNA and amino acid sequence determination and analysis, functional expression of AtCKX2 and AtCKX4 in Pichia pastoris, Physcomitrella patens, and Saccharomyces cerevisiae, the recombinant enzymes are located in protoplasts or are secreted to the medium, overview, phylogenetic analysis
expressed in Escherichia coli strain DH5alpha
expressed in in Arabidopsis thaliana Ler suspension culture
expressed in Physcomitrella patens protoplasts, expression of the AtCKX2 gene results in an up to 27fold increase of activity compared with wild type Physcomitrella patens, expression of AtCKX2 results in a significant decrease of cytokinin level and morphological changes such as altered morphology of filaments, impaired budding, and loss of sexual reproductivity
expression of cytosolic isozyme AtCKX7 in Escherichia coli and intracellularly in Pichia pastoris
expression of vacuolar His-tagged isozyme AtCKX1 in Pichia pastoris
gene DsCKX1, DNA and amino acid sequence determination and analysis, analysis of expression, regulation, phylogenetic analysis
gene FasV of RfCKX1, expression as polycistronic mRNA, fas operon, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene HvCKX2, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae, transformation and overexpression in Arabidopsis thaliana and Nicotiana tabacum using the Agrobacterium tumefaciens strain GUS3101 system
gene HvCKX2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene HvCKX3, DNA and amino acid sequence determination and analysis, expression in Saccharomyces cerevisiae, transformation and overexpression in Arabidopsis thaliana and Nicotiana tabacum using the Agrobacterium tumefaciens strain GUS3101 system
gene NsCKX1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
-
gene TaCKX3, DNA and amino acid sequence determination and analysis, phylogenetic tree
gene ZmCKX1, DNA and amino acid sequence determination and analysis, functional expression in Pichia pastoris, Physcomitrella patens, and Saccharomyces cerevisiae, phylogenetic analysis
high-level expression of cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
24-epibrassinolide inhibits both cytokinin oxidase activity and expression. Treatment with 0.4 mM 24-epibrassinolide leads to elevated cytokinin levels in roots and shoots, that are maintained only in the presence of 24-epibrassinolide, while the hormone removal leads to return of cytokinin concentration to the control level initially in the roots and then in the shoots
expression is upregulated by N-(2-chloro-4-pyridyl)-N'-phenylurea
expression is upregulated in presence of N-(2-chloro-4-pyridyl)-N'-phenylurea
highest levels of the CKX1 transcript are detected in spikes 0 days, 7 days, and 14 days after pollination and in the seedling roots
highly expressed in inflorescence
light promotes an 8fold increase of cytokinin oxidase/dehydrogenase activity within the first 4 days of incubation under a light/dark regime of 18 h white light and 6 h darkness. The CKX activity reaches a high maximum when the plants have an age of 36 d
-
light promotes an increase of cytokinin oxidase/dehydrogenase activity within the first 4 days of incubation under a light/dark regime of 18 h white light and 6 h darkness
24-epibrassinolide inhibits both cytokinin oxidase activity and expression. Treatment with 0.4 mM 24-epibrassinolide leads to elevated cytokinin levels in roots and shoots, that are maintained only in the presence of 24-epibrassinolide, while the hormone removal leads to return of cytokinin concentration to the control level initially in the roots and then in the shoots
-
24-epibrassinolide inhibits both cytokinin oxidase activity and expression. Treatment with 0.4 mM 24-epibrassinolide leads to elevated cytokinin levels in roots and shoots, that are maintained only in the presence of 24-epibrassinolide, while the hormone removal leads to return of cytokinin concentration to the control level initially in the roots and then in the shoots
-
-
highest levels of the CKX1 transcript are detected in spikes 0 days, 7 days, and 14 days after pollination and in the seedling roots
highest levels of the CKX1 transcript are detected in spikes 0 days, 7 days, and 14 days after pollination and in the seedling roots
-
light promotes an increase of cytokinin oxidase/dehydrogenase activity within the first 4 days of incubation under a light/dark regime of 18 h white light and 6 h darkness
-
light promotes an increase of cytokinin oxidase/dehydrogenase activity within the first 4 days of incubation under a light/dark regime of 18 h white light and 6 h darkness
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
reduced expression of OsCKX2 causes cytokinin accumulation in inflorescence meristems and increases the number of reproductive organs, resulting in enhanced grain yield. Quantitative trait loci pyramiding to combine loci for grain number and plant heigh in the same genetic background generates lines exhibiting both beneficial traits. The results provide a strategy for tailormade crop improvement
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Galuszka, P.; Frebort, I.; Sebela, M.; Sauer, P.; Jacobsen, S.; Pec, P.
Cytokinin oxidase or dehydrogenase? Mechanism of cytokinin degradation in cereals
Eur. J. Biochem.
268
450-461
2001
Hordeum vulgare, Triticum aestivum
brenda
Burch, L.R.; Horgan, R.
The purification of cytokinin oxidase from Zea mays kernels
Phytochemistry
28
1313-1319
1989
Triticum aestivum, Zea mays
-
brenda
McGaw, B.A.; Horgan, R.
Cytokinin catabolism and cytokinin oxidase
Phytochemistry
22
1103-1105
1983
Zea mays
-
brenda
Motyka, V.; Faiss, M.; Strnad, M.; Kaminek, M.; Schmuelling, T.
Changes in cytokinin content and cytokinin oxidase activity in response to derepression of ipt gene transcription in transgenic tobacco calli and plants
Plant Physiol.
112
1035-1043
1996
Nicotiana tabacum
brenda
Chatfield, J.M.; Armstrong, D.J.
Cytokinin oxidase from Phaseolus vulgaris callus tissues. Enhanced in vitro activity of the enzyme in the presence of copper-imidazole complexes
Plant Physiol.
84
726-731
1987
Phaseolus vulgaris
brenda
Bilyeu, K.D.; Cole, J.L.; Laskey, J.G.; Riekhof, W.R.; Esparza, T.J.; Kramer, M.D.; Morris, R.O.
Molecular and biochemical characterization of a cytokinin oxidase from maize
Plant Physiol.
125
378-386
2001
Zea mays
brenda
Chatfield, J.M.; Armstrong, D.J.
Regulation of cytokinin oxidase activity in callus tissues of Phaseolus vulgaris L. cv Great Northern
Plant Physiol.
80
493-499
1986
Phaseolus vulgaris
brenda
Galuszka, P.; Frebort, I.; Sebela, M.; Pec, P.
Degradation of cytokinins by cytokinin oxidases in plants
Plant Growth Regul.
32
315-327
2000
Triticum aestivum, Zea mays, Nicotiana tabacum, Phaseolus lunatus, Catharanthus roseus, Populus x canadensis
-
brenda
Hare, P.D.; van Staden, J.
Cytokinin oxidase: biochemical features and physiological significance
Physiol. Plant.
91
128-136
1994
Triticum aestivum, Zea mays, Nicotiana tabacum, Phaseolus vulgaris, Phaseolus lunatus, Catharanthus roseus, Populus x canadensis, Glycine max
-
brenda
Dietrich, J.T.; Kaminek, M.; Blevins, D.G.; Reinbott, T.M.; Morris, R.O.
Changes in cytokinins and cytokinin oxidase activity in developing maize kernels and the effects of exogenous cytokinin on kernel development
Plant Physiol. Biochem.
33
327-336
1995
Zea mays
-
brenda
Auer, C.A.; Motyka, V.; Brezinova, A.; Kaminek, M.
Endogenous cytokinin accumulation and cytokinin oxidase activity during shoot organogenesis of Petunia hybrida
Physiol. Plant.
105
141-147
1999
Petunia x hybrida
-
brenda
Wang, J.; Letham, D.S.
Cytokinin oxidase - purification by affinity chromatography and activation by caffeic acid
Plant Sci.
112
161-166
1995
Nicotiana tabacum
-
brenda
Kopecny, D.; Briozzo, P.; Joly, N.; Houba-Herin, N.; Madzak, C.; Pethe, C.; Laloue, M.
Purification, crystallization and preliminary X-ray diffraction study of a recombinant cytokinin oxidase from Zea mays
Acta Crystallogr. Sect. D
60
1500-1501
2004
Zea mays
brenda
Frebortova, J.; Fraaije, M.W.; Galuszka, P.; Sebela, M.; Pec, P.; Hrbac, J.; Novak, O.; Bilyeu, K.D.; English, J.T.; Frebort, I.
Catalytic reaction of cytokinin dehydrogenase: preference for quinones as electron acceptors
Biochem. J.
380
121-130
2004
Zea mays (Q9T0N8), Zea mays
brenda
Galuszka, P.; Frebortova, J.; Werner, T.; Yamada, M.; Strnad, M.; Schmulling, T.; Frebort, I.
Cytokinin oxidase/dehydrogenase genes in barley and wheat: cloning and heterologous expression
Eur. J. Biochem.
271
3990-4002
2004
Hordeum vulgare, Hordeum vulgare (Q8H6F6), Hordeum vulgare (Q84U27), Hordeum vulgare (Q94KI4), Triticum aestivum (Q94KI5), Triticum aestivum
brenda
Malito, E.; Coda, A.; Bilyeu, K.D.; Fraaije, M.W.; Mattevi, A.
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis
J. Mol. Biol.
341
1237-1249
2004
Zea mays (Q9T0N8), Zea mays
brenda
Schmulling, T.; Werner, T.; Riefler, M.; Krupkova, E.; Bartrina y Manns, I.
Structure and function of cytokinin oxidase/dehydrogenase genes of maize, rice, Arabidopsis and other species
J. Plant Res.
116
241-252
2003
Arabidopsis thaliana (Q9FUJ3), Arabidopsis thaliana, Dendrobium hybrid cultivar (Q9FE45), Dictyostelium discoideum, Hordeum vulgare (Q8H6F6), Nicotiana tabacum, no activity in Physcomitrella patens, no activity in Pichia pastoris, no activity in Prochlorococcus marinus, no activity in Raphanus sativus, no activity in Saccharomyces cerevisiae, no activity in Synechocystis sp., no activity in Synechocystis sp. PCC 6803, Nostoc sp., Oryza sativa, Phaseolus sp., Rhodococcoides fascians, Zea mays (Q9T0N8), Zea mays
brenda
Motyka, V.; Vankova, R.; Capkova, V.; Petrasek, J.; Kaminek, M.; Schmulling, T.
Cytokinin-induced upregulation of cytokinin oxidase activity in tobacco includes changes in enzyme glycosylation and secretion
Physiol. Plant.
117
11-21
2003
Nicotiana tabacum
-
brenda
Galuszka, P.; Frebortova, J.; Luhova, L.; Bilyeu, K.D.; English, J.T.; Frebort, I.
Tissue localization of cytokinin dehydrogenase in maize: possible involvement of quinone species generated from plant phenolics by other enzymatic systems in the catalytic reaction
Plant Cell Physiol.
46
716-728
2005
Zea mays (Q9T0N8), Zea mays, Zea mays ZmCKX1 (Q9T0N8)
brenda
Laskey, J.G.; Patterson, P.; Bilyeu, K.; Morris, R.O.
Rate enhancement of cytokinin oxidase/dehydrogenase using 2,6-dichlorophenolindophenol as an electron acceptor
Plant Growth Regul.
40
189-196
2003
Zea mays
-
brenda
Vaseva-Gemisheva, I.; Lee, D.; Alexieva, V.; Karanov, E.
Cytokinin oxidase/dehydrogenase in Pisum sativum plants during vegetative development. Influence of UV-B irradiation and high temperature on enzymatic activity
Plant Growth Regul.
42
1-5
2004
Lathyrus oleraceus
-
brenda
Blagoeva, E.; Dobrev, P.I.; Malbeck, J.; Motyka, V.; Gaudinova, A.; Vankova, R.
Effect of exogenous cytokinins, auxins and adenine on cytokinin N-glucosylation and cytokinin oxidase/dehydrogenase activity in de-rooted radish seedlings
Plant Growth Regul.
44
15-23
2004
Raphanus sativus
-
brenda
Popelkova, H.; Fraaije, M.W.; Novak, O.; Frebortova, J.; Bilyeu, K.D.; Frebort, I.
Kinetic and chemical analyses of the cytokinin dehydrogenase-catalysed reaction: correlations with the crystal structure
Biochem. J.
398
113-124
2006
Zea mays
brenda
Kopecny, D.; Pethe, C.; Sebela, M.; Houba-Herin, N.; Madzak, C.; Majira, A.; Laloue, M.
High-level expression and characterization of Zea mays cytokinin oxidase/dehydrogenase in Yarrowia lipolytica
Biochimie
87
1011-1022
2005
Zea mays (Q9T0N8), Zea mays
brenda
Novakova, M.; Motyka, V.; Dobrev, P.I.; Malbeck, J.; Gaudinova, A.; Vankova, R.
Diurnal variation of cytokinin, auxin and abscisic acid levels in tobacco leaves
J. Exp. Bot.
56
2877-2883
2005
Nicotiana tabacum
brenda
Gaudinova, A.; Dobrev, P.I.; Solcova, B.; Novak, O.; Strnad, M.; Friedecky, D.; Motyka, V.
The involvement of cytokinin oxidase/dehydrogenase and zeatin reductase in regulation of cytokinin levels in pea (Pisum sativum L.) leaves
J. Plant Growth Regul.
24
188-200
2005
Lathyrus oleraceus
-
brenda
Sriskandarajah, S.; Prinsen, E.; Motyka, V.; Dobrev, P.I.; Serek, M.
Regenerative capacity of cacti Schlumbergera and Rhipsalidopsis in relation to endogenous phytohormones, cytokinin oxidase/dehydrogenase, and peroxidase activities
J. Plant Growth Regul.
25
79-88
2006
Rhipsalidopsis sp., Schlumbergera sp.
-
brenda
Suttle, J.C.; Mornet, R.
Mechanism-based irreversible inhibitors of cytokinin dehydrogenase
J. Plant Physiol.
162
1189-1196
2005
Solanum tuberosum
brenda
Ashikari, M.; Sakakibara, H.; Lin, S.; Yamamoto, T.; Takashi, T.; Nishimura, A.; Angeles, E.R.; Qian, Q.; Kitano, H.; Matsuoka, M.
Cytokinin oxidase regulates rice grain production
Science
309
741-745
2005
Oryza sativa
brenda
Ananieva, K.I.; Stirk, W.A.; Kaminek, M.; van Staden, J.
Some biochemical properties of cytokinin oxidase/dehydrogenase in Cucurbita pepo L. (zucchini) leaves
South Afr. J. Bot.
71
253-256
2005
Cucurbita pepo
-
brenda
Valdes, A.E.; Galuszka, P.; Fernandez, B.; Centeno, M.L.; Frebort, I.
Developmental stage as a possible factor affecting cytokinin content and cytokinin dehydrogenase activity in Pinus sylvestris
Biol. Plant.
51
193-197
2007
Pinus sylvestris
-
brenda
Todorova, D.; Vaseva, I.; Malbeck, J.; Travnickova, A.; Machackova, I.; Karanov, E.
Cytokinin oxidase/dehydrogenase activity as a tool in gibberellic acid/cytokinin cross talk
Biol. Plant.
51
579-583
2007
Lathyrus oleraceus (A0MQ40)
-
brenda
Frebortova, J.; Galuszka, P.; Werner, T.; Schmulling, T.; Frebort, I.
Functional expression and purification of cytokinin dehydrogenase from Arabidopsis thaliana (AtCKX2) in Saccharomyces cerevisiae
Biol. Plant.
51
673-682
2007
Arabidopsis thaliana
-
brenda
Carabelli, M.; Possenti, M.; Sessa, G.; Ciolfi, A.; Sassi, M.; Morelli, G.; Ruberti, I.
Canopy shade causes a rapid and transient arrest in leaf development through auxin-induced cytokinin oxidase activity
Genes Dev.
21
1863-1868
2007
Arabidopsis thaliana
brenda
Kopecny, D.; Sebela, M.; Briozzo, P.; Spichal, L.; Houba-Herin, N.; Masek, V.; Joly, N.; Madzak, C.; Anzenbacher, P.; Laloue, M.
Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor
J. Mol. Biol.
380
886-899
2008
Zea mays (Q9T0N8), Zea mays
brenda
Held, M.; Pepper, A.N.; Bozdarov, J.; Smith, M.D.; Emery, R.J.; Guinel, F.C.
The pea nodulation mutant R50 (sym16) displays altered activity and expression profiles for cytokinin dehydrogenase
J. Plant Growth Regul.
27
170-180
2008
Lathyrus oleraceus (A0MQ40)
-
brenda
Conrad, K.; Motyka, V.; Schlueter, T.
Increase in activity, glycosylation and expression of cytokinin oxidase/dehydrogenase during the senescence of barley leaf segments in the dark
Physiol. Plant.
130
572-579
2007
Hordeum vulgare
-
brenda
von Schwartzenberg, K.; Nunez, M.F.; Blaschke, H.; Dobrev, P.I.; Novak, O.; Motyka, V.; Strnad, M.
Cytokinins in the bryophyte Physcomitrella patens: Analyses of activity, distribution, and cytokinin oxidase/dehydrogenase overexpression reveal the role of extracellular cytokinins
Plant Physiol.
145
786-800
2007
Physcomitrium patens, Arabidopsis thaliana (Q9FUJ3)
brenda
Bae, E.; Bingman, C.A.; Bitto, E.; Aceti, D.J.; Phillips, G.N.
Crystal structure of Arabidopsis thaliana cytokinin dehydrogenase
Proteins
70
303-306
2007
Arabidopsis thaliana (Q9FUJ1), Arabidopsis thaliana
brenda
Zatloukal, M.; Gemrotova, M.; Dolezal, K.; Havlicek, L.; Spichal, L.; Strnad, M.
Novel potent inhibitors of A. thaliana cytokinin oxidase/dehydrogenase
Bioorg. Med. Chem.
16
9268-9275
2008
Arabidopsis thaliana
brenda
Smehilova, M.; Galuszka, P.; Bilyeu, K.D.; Jaworek, P.; Kowalska, M.; Sebela, M.; Sedlarova, M.; English, J.T.; Frebort, I.
Subcellular localization and biochemical comparison of cytosolic and secreted cytokinin dehydrogenase enzymes from maize
J. Exp. Bot.
60
2701-2712
2009
Zea mays (Q9T0N8), Zea mays (B6V8F7), Zea mays
brenda
Wang, Y.; Luo, J.P.; Wei, Z.J.; Zhang, J.C.
Molecular cloning and expression analysis of a cytokinin oxidase (DhCKX) gene in Dendrobium huoshanense
Mol. Biol. Rep.
36
1331-1338
2008
Dendrobium huoshanense (A2TLJ3), Dendrobium huoshanense
brenda
Ananieva, K.; Ananiev, E.D.; Doncheva, S.; Georgieva, K.; Tzvetkova, N.; Kaminek, M.; Motyka, V.; Dobrev, P.; Gajdosova, S.; Malbeck, J.
Senescence progression in a single darkened cotyledon depends on the light status of the other cotyledon in Cucurbita pepo (zucchini) seedlings: potential involvement of cytokinins and cytokinin oxidase/dehydrogenase activity
Physiol. Plant.
134
609-623
2008
Cucurbita pepo
brenda
Kopecny, D.; Briozzo, P.; Popelkova, H.; Sebela, M.; Koncitikova, R.; Spichal, L.; Nisler, J.; Madzak, C.; Frebort, I.; Laloue, M.; Houba-Herin, N.
Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study
Biochimie
92
1052-1062
2010
Zea mays (Q9T0N8), Zea mays
brenda
Zalewski, W.; Galuszka, P.; Gasparis, S.; Orczyk, W.; Nadolska-Orczyk, A.
Silencing of the HvCKX1 gene decreases the cytokinin oxidase/dehydrogenase level in barley and leads to higher plant productivity
J. Exp. Bot.
61
1839-1851
2010
Hordeum vulgare (Q94KI4), Hordeum vulgare, Triticum aestivum
brenda
Schlueter, T.; Leide, J.; Conrad, K.
Light promotes an increase of cytokinin oxidase/dehydrogenase activity during senescence of barley leaf segments
J. Plant Physiol.
168
694-698
2011
Hordeum vulgare, Phragmites australis, Zea mays
brenda
Frebortova, J.; Novak, O.; Frebort, I.; Jorda, R.
Degradation of cytokinins by maize cytokinin dehydrogenase is mediated by free radicals generated by enzymatic oxidation of natural benzoxazinones
Plant J.
61
467-481
2010
Zea mays
brenda
Saravanakumar, A.; Aslam, A.; Shajahan, A.
Histochemical localization of cytokinin oxidase/dehydrogenase during the developmental stages of Withania somnifera (L.) Dunal
Afr. J. Biotechnol.
10
8800-8804
2011
Withania somnifera
-
brenda
Avalbaev, A.M.; Somov, K.A.; Yuldashev, R.A.; Shakirova, F.M.
Cytokinin oxidase is key enzyme of cytokinin degradation
Biochemistry (Moscow)
77
1354-1361
2012
Arabidopsis thaliana, Nicotiana tabacum, Zea mays, Oryza sativa, Populus sp., Physcomitrium patens, Selaginella moellendorffii, Hordeum vulgare
brenda
Cueno, M.E.; Imai, K.; Ochiai, K.; Okamoto, T.
Cytokinin dehydrogenase differentially regulates cytokinin and indirectly affects hydrogen peroxide accumulation in tomato leaf
J. Plant Physiol.
169
834-838
2012
Solanum lycopersicum, Solanum lycopersicum Improved Pope
brenda
Kowalska, M.; Galuszka, P.; Frebortova, J.; Sebela, M.; Beres, T.; Hluska, T.; Smehilova, M.; Bilyeu, K.D.; Frebort, I.
Vacuolar and cytosolic cytokinin dehydrogenases of Arabidopsis thaliana: heterologous expression, purification and properties
Phytochemistry
71
1970-1978
2010
Arabidopsis thaliana, Arabidopsis thaliana (O22213), Arabidopsis thaliana (Q9LTS3)
brenda
Ma, X.; Feng, D.; Wang, H.; Li, X.; Kong, L.
Cloning and expression analysis of wheat cytokinin oxidase/dehydrogenase gene TaCKX3
Plant Mol. Biol. Rep.
29
98-105
2011
Triticum aestivum (D3JAJ5), Triticum aestivum Yanyou 361 (D3JAJ5)
-
brenda
Yuldashev, R.; Avalbaev, A.; Bezrukova, M.; Vysotskaya, L.; Khripach, V.; Shakirova, F.
Cytokinin oxidase is involved in the regulation of cytokinin content by 24-epibrassinolide in wheat seedlings
Plant Physiol. Biochem.
55
1-6
2012
Triticum aestivum, Triticum aestivum Bashkirskaya 24
brenda
Vysotskaya, L.; Avalbaev, A.; Yuldashev, R.; Shakirova, F.; Veselov, S.; Kudoyarova, G.
Regulation of cytokinin oxidase activity as a factor affecting the content of cytokinins
Russ. J. Plant Physiol.
57
494-500
2010
Triticum turgidum subsp. durum, Triticum turgidum subsp. durum Bezenchukskaya 139
-
brenda
Frebortova, J.; Greplova, M.; Seidl, M.F.; Heyl, A.; Frebort, I.
Biochemical characterization of putative adenylate dimethylallyltransferase and cytokinin dehydrogenase from Nostoc sp. PCC 7120
PLoS ONE
10
e0138468
2015
no activity in Nostoc sp. PCC 7120
brenda
Marques, M.; Freitas, B.; Guedes, T.; Fernandes, R.
Cytokinin dehydrogenase activity in primary roots and characterization of primary metabolites from leaves and rootlets of Ricinus communis
Braz. Arch. Biol. Technol.
56
904-910
2013
Ricinus communis
-
brenda
Ma, Y.; Zheng, L.; Xie, R.; He, S.; Deng, L.
Genome-wide identification and analysis of CKX genes in Poncirus trifoliata
J. Hortic. Sci. Biotechnol.
91
592-602
2016
Citrus trifoliata
-
brenda
Pospisilova, H.; Jiskrova, E.; Vojta, P.; Mrizova, K.; Kokas, F.; Cudejkova, M.M.; Bergougnoux, V.; Plihal, O.; Klimesova, J.; Novak, O.; Dzurova, L.; Frebort, I.; Galuszka, P.
Transgenic barley overexpressing a cytokinin dehydrogenase gene shows greater tolerance to drought stress
New Biotechnol.
33
692-705
2016
Arabidopsis thaliana (O22213), Arabidopsis thaliana
brenda
Zalabak, D.; Johnova, P.; Plihal, O.; Senkova, K.; Samajova, O.; Jiskrova, E.; Novak, O.; Jackson, D.; Mohanty, A.; Galuszka, P.
Maize cytokinin dehydrogenase isozymes are localized predominantly to the vacuoles
Plant Physiol. Biochem.
104
114-124
2016
Zea mays, Zea mays (Q9T0N8), Zea mays (B6V8F7), Zea mays (E3T1X0), Zea mays (E3T1X1), Zea mays (E3T1X2), Zea mays (E3T1X3)
brenda
Zalabak, D.; Galuszka, P.; Mrizova, K.; Podle?akova, K.; Gu, R.; Frebortova, J.
Biochemical characterization of the maize cytokinin dehydrogenase family and cytokinin profiling in developing maize plantlets in relation to the expression of cytokinin dehydrogenase genes
Plant Physiol. Biochem.
74
283-293
2014
Zea mays, Zea mays (Q9T0N8), Zea mays (E3T1X1)
brenda
Mrizova, K.; Jiskrova, E.; Vyroubalova, S.; Novak, O.; Ohnoutkova, L.; Pospisilova, H.; Frebort, I.; Harwood, W.A.; Galuszka, P.
Overexpression of cytokinin dehydrogenase genes in barley (Hordeum vulgare cv. Golden Promise) fundamentally affects morphology and fertility
PLoS ONE
8
e79029
2013
Hordeum vulgare (I3VIX5), Hordeum vulgare
brenda
Tian, F.; Greplova, M.; Frebort, I.; Dale, N.; Napier, R.
A highly selective biosensor with nanomolar sensitivity based on cytokinin dehydrogenase
PLoS ONE
9
e90877
2014
Zea mays (Q9T0N8), Zea mays
brenda
Tsago, Y.; Chen, Z.; Cao, H.; Sunusi, M.; Khan, A.; Shi, C.; Jin, X.
Rice gene, OsCKX2-2, regulates inflorescence and grain size by increasing endogenous cytokinin content
Plant Growth Regul.
92
283-294
2020
Oryza sativa Japonica Group (Q4ADV8)
-
brenda
Czajkowska, B.; Finlay, C.; Jones, G.; Brown, T.
Diversity of a cytokinin dehydrogenase gene in wild and cultivated barley
PLoS ONE
14
e0225899
2019
Hordeum vulgare
brenda
Yu, K.; Yu, Y.; Bian, L.; Ni, P.; Ji, X.; Guo, D.; Zhang, G.; Yang, Y.
Genome-wide identification of cytokinin oxidases/dehydrogenase (CKXs) in grape and expression during berry set
Sci. Hortic.
280
109917
2021
Vitis vinifera (D7TS26), Vitis vinifera (F6H3S4), Vitis vinifera (F6HZZ3), Vitis vinifera (D7U3H6), Vitis vinifera (F6HGV7), Vitis vinifera (F6HHY5), Vitis vinifera (F6H1K3), Vitis vinifera (D7TSA7)
-
brenda
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