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cis-zeatin + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
cis/trans-zeatin riboside + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
N6-(2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenine + 1,4-naphthoquinone
adenine + 3-methylbut-2-enal + reduced 1,4-naphthoquinone
-
-
-
?
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
i.e. coenzyme Q0
-
-
?
N6-(2-isopentenyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
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 + caffeic acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + coenzyme Q1
adenine + 3-methylbut-2-enal + reduced coenzyme Q1
-
-
-
?
N6-(2-isopentenyl)adenine + cytochrome c
adenine + 3-methylbut-2-enal + reduced cytochrome c
-
-
-
?
N6-(2-isopentenyl)adenine + daphnoretin
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-(2-isopentenyl)adenine + o-coumaric acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + O2
adenine + 3-methylbut-2-enal + H2O2
oxidative degradation of cytokinins, slow reaction, low substrate specificity
-
-
?
N6-(2-isopentenyl)adenine + plantacyanine
adenine + 3-methylbut-2-enal + reduced plantacyanine
electron acceptor from spinach
-
-
?
N6-(2-isopentenyl)adenine + rosmarinic acid
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + scopoletin
adenine + 3-methylbut-2-enal + ?
-
-
-
?
N6-(2-isopentenyl)adenine + spinach plantacyanine
adenine + 3-methylbut-2-enal + reduced spinach plantacyanine
-
-
-
r
N6-(2-isopentenyl)adenine + vitamin K1
adenine + 3-methylbut-2-enal + reduced vitamin K1
-
-
-
?
N6-(2-isopentenyl)adenine + vitamin K3
adenine + 3-methylbut-2-enal + reduced vitamin K3
-
-
-
?
N6-(2-isopentenyl)adenosine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(2-isopentenyl)adenosine + FAD
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(4-hydroxy-2-butynyl)adenine + 2,6-dichlorophenol indophenol
?
very effective electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenine + 4-methylcatechol + H2O
adenine + 3-methylbut-2-enal + reduced 4-methylcatechol
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + acetosyringone + H2O
adenine + 3-methylbut-2-enal + reduced acetosyringone
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
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
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 2,6-dichlorophenolindophenol + H2O
adenosine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
artificial electron acceptor
-
-
?
N6-(DELTA2-isopentenyl)adenosine + 4-methylcatechol + H2O
adenosine + 3-methylbut-2-enal + reduced 4-methylcatechol
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + acetosyringone + H2O
adenosine + 3-methylbut-2-enal + reduced acetosyringone
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + guaiacol + H2O
adenosine + 3-methylbut-2-enal + reduced guaiacol
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-benzyladenine + FAD + H2O
adenine + ? + FADH2
substrate binding mechanism and structure, overview
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-dimethylallyladenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
i.e. isopentenyladenosine
-
-
ir
N6-isopentenyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methyl-2-butenal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-isopentenyladenine + oxidized 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenosine + 2,6-dichlorophenolindophenol
3-methylbut-2-enal + adenosine + reduced 2,6-dichlorophenolindophenol
-
-
-
?
N6-isopentenyladenosine + oxidized 2,6-dichlorophenolindophenol
adenosine + 3-methylbut-2-enol + reduced 2,6-dichlorophenolindophenol
-
-
-
?
trans-zeatin + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
trans-zeatin + FAD + H2O
? + FADH2
substrate binding mechanism and structure, overview
-
-
ir
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
trans-zeatin riboside + 2,6-dichlorophenolindophenol + H2O
?
most favorable substrate
-
-
?
zeatin + 2,6-dichlorophenolindophenol
4-hydroxy-3-methylbut-2-enal + adenine + reduced 2,6-dichlorophenolindophenol
-
-
-
?
zeatin + FAD
? + FADH2
-
-
-
?
zeatin + FAD + H2O
adenine + 4-hydroxy-3-methylbut-2-enal + FADH2
-
-
-
ir
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
cis-zeatin + acceptor + H2O
?
cis-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
kinetin + FAD
2-furaldehyde + adenine + FADH2
-
-
-
-
?
N-methyl-isopentenyladenine + FAD
?
-
-
-
-
?
N6-(2-isopentenyl)adenine + 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) radical + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
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
-
4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
-
-
?
N6-(2-isopentenyl)adenine + 4-nitrosoresorcinol-1-monomethyl ether + H2O
adenine + 3-methylbut-2-enal + reduced 4-nitrosoresorcinol-1-monomethyl ether
-
4-nitrosoresorcinol-1-monomethyl ether serves as a weak electron acceptor of CKX
-
-
?
N6-(2-isopentenyl)adenine + CuCl2 + H2O
adenine + 3-methylbut-2-enal + ?
-
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
-
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
-
-
?
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
-
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
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
N6-(DELTA2-isopentenyl)adenine-9-beta-D-glucoside + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine-5'-monophosphate + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-dimethylallyladenine + 2,6-dichlorophenolindophenol
adenine + 3-methylbut-2-enal + reduced 2,6-dichlorophenolindophenol
-
i.e. isopentenyladenine, reaction via an imine intermediate
-
-
?
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
?
N6-dimethylallyladenine + FAD + H2O2
adenine + 3-methylbut-2-enal + FADH2 + O2
-
i.e. isopentenyladenine
-
-
?
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
-
-
-
?
N6-isopentenyladenosine + electron acceptor
3-methylbut-2-enal + adenosine + reduced electron acceptor
-
-
-
-
?
O-beta-D-glucosyl-trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
p-topolin + FAD
?
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
trans-zeatin + electron acceptor
(2E)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
trans-zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
-
?
trans-zeatin + oxidized 2,6-dichlorophenolindophenol
?
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
-
-
-
ir
cis/trans-zeatin + FAD + H2O
adenine + ? + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(2-isopentenyl)adenine + FAD
adenine + 3-methylbut-2-enal + FADH2
the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
preferred substrate
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
i.e. isopentenyladenine
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
oxidative degradation
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
substrate binding mechanism and structure, overview
-
-
ir
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
?
zeatin riboside + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
cis-zeatin + acceptor + H2O
?
-
-
-
-
?
cis-zeatin + acceptor + H2O
?
-
preferred substrate of isozyme ZmCKX10
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + 2,6-dichlorophenolindophenol + H2O
?
-
-
-
?
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
oxidative degradation of cytokinins
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
?
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
-
-
ir
N6-isopentenyladenine + electron acceptor
adenine + 3-methyl-2-butenal + reduced electron acceptor
-
FAD is cofactor
-
ir
trans-zeatin + acceptor + H2O
?
-
-
-
-
?
trans-zeatin + acceptor + H2O
?
-
preferred substrate of isozymes ZmCKX1 and ZmCKX10
-
-
?
additional information
?
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
-
enzyme expression is co-localized with laccase, enzyme activity probably is associated with plant phenolic oxidation
-
-
?
additional information
?
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
-
enzyme has a major role in control of cytokinin plant hormone levels
-
-
?
additional information
?
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
-
enzyme has a regulatory role in cytokinin metabolism and cytokinin-dependent processes, influences chloroplast development
-
-
?
additional information
?
-
specificity for electron acceptors, overview
-
-
?
additional information
?
-
-
specificity for electron acceptors, overview
-
-
?
additional information
?
-
substrate specificity with cytokinins, overiew
-
-
?
additional information
?
-
-
substrate specificity with cytokinins, overiew
-
-
?
additional information
?
-
the substrate binding site is located at amino acid residues 245-491
-
-
?
additional information
?
-
-
the substrate binding site is located at amino acid residues 245-491
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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0.004 - 0.009
(2,6-dichloro-pyridin-4-yl)-carbamic acid benzyl ester
0.0002 - 0.039
(2-chloro-pyridin-4-yl)-carbamic acid 4-chloro-phenyl ester
0.005 - 0.13
1-(2-chloro-1-oxidopyridin-4-yl)-3-phenylurea
0.0001 - 0.006
1-imidazo[1,2-a]pyridin-7-yl-3-phenylurea
0.005 - 0.05
N-(1,2,3-thidiazol-5-yl)-N'-phenylurea
0.002 - 0.009
N-(2,6-dichloro-pyridin-4-yl)-N'-benzylurea
0.005 - 0.02
N-(2,6-dichloro-pyridin-4-yl)-N'-phenoxyurea
0.00008 - 0.0045
N-(2,6-dichloro-pyridin-4-yl)-N'-phenylurea
0.0011 - 0.002
N-(2,6-dichloropyridin-4-yl)-N'-benzyl-N'-methylurea
0.006 - 0.032
N-(2-amino-6-chloro-pyridin-4-yl)-N'-benzylurea
0.00004 - 0.0018
N-(2-amino-6-chloro-pyridin-4-yl)-N'-phenylurea
0.00004 - 0.035
N-(2-amino-pyridin-4-yl)-N'-phenylurea
0.006 - 0.022
N-(2-chloro-6-methoxy-pyridin-4-yl)-N'-benzylurea
0.0015 - 0.018
N-(2-chloro-pyridin-4-yl)-N'-benzylurea
0.035 - 0.055
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
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 E381S, 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
0.009
(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 E381A, 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
0.008
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
mutant enzyme E381S, 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
0.006
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
0.055
N-(2-chloro-pyridin-4-yl)-N'-phenylurea
Zea mays
mutant enzyme E381S, pH and temperature not specified in the publication
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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
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
Galuszka, P.; Frebort, I.; Sebela, M.; Pec, P.
Degradation of cytokinins by cytokinin oxidases in plants
Plant Growth Regul.
32
315-327
2000
Catharanthus roseus, Nicotiana tabacum, Phaseolus lunatus, Populus x canadensis, Triticum aestivum, Zea mays
-
brenda
Hare, P.D.; van Staden, J.
Cytokinin oxidase: biochemical features and physiological significance
Physiol. Plant.
91
128-136
1994
Catharanthus roseus, Glycine max, Nicotiana tabacum, Phaseolus lunatus, Phaseolus vulgaris, Populus x canadensis, Triticum aestivum, Zea mays
-
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
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
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., Rhodococcus fascians, Zea mays (Q9T0N8), Zea mays
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
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
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
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 (B6V8F7), Zea mays (Q9T0N8), Zea mays
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
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
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, Hordeum vulgare, Nicotiana tabacum, Oryza sativa, Physcomitrium patens, Populus sp., Zea mays, Selaginella moellendorffii
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 (B6V8F7), Zea mays (E3T1X0), Zea mays (E3T1X1), Zea mays (E3T1X2), Zea mays (E3T1X3), Zea mays (Q9T0N8)
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 (E3T1X1), Zea mays (Q9T0N8)
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