Any feedback?
Information on EC 1.5.99.12 - cytokinin dehydrogenase and Organism(s) Zea mays and UniProt Accession Q9T0N8
for references in articles please use BRENDA:EC1.5.99.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.5.99.12 cytokinin dehydrogenaseIUBMB 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 .
Specify your search results
Word Map
- 1.5.99.12
- trans-zeatin
- riboside
- cis-zeatin
-
isopentenyltransferase
-
cytokinin-deficient
- agriculture
The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
cytokinin oxidase, cytokinin oxidase/dehydrogenase, cytokinin dehydrogenase, osckx2, hvckx1, zmckx1, zmcko1, atckx2, atckx7, atckx3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CKX1
cytokinin oxidase
isopentenyladenosine oxidase
-
-
-
-
N6-(D2-isopentenyl)adenosine oxidase
-
-
-
-
N6-isopentenylaldenine oxidase
-
-
-
-
zeatin oxidase
-
-
-
-
cytokinin oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N6-dimethylallyladenine + acceptor + H2O = adenine + 3-methylbut-2-enal + reduced acceptor
N6-dimethylallyladenine + 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-dimethylallyladenine + 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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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].
CAS REGISTRY NUMBER
COMMENTARY
55326-39-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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
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-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 + 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 + FAD + H2O
? + FADH2
substrate binding mechanism and structure, overview
-
-
ir
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
-
-
-
?
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 + 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-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 + 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
?
-
-
-
?
trans-zeatin + electron acceptor
(2E)-4-hydroxy-3-methylbut-2-enal + adenine + reduced electron acceptor
-
-
-
-
?
zeatin + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
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
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
-
-
-
-
?
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
?
-
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
?
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
the natural terminal electron acceptor probably is a p-quinone or a similar compound, high substrate specificity for N6-(2-isopentenyl)adenine
-
-
?
N6-(2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-(DELTA2-isopentenyl)adenosine + FAD + H2O
adenosine + 3-methylbut-2-enal + FADH2
-
-
-
?
N6-dimethylallyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
enzyme catalyzes the irreversible degradation of cytokinins
-
-
ir
N6-isopentenyladenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
oxidative degradation
-
-
ir
N6-(DELTA2-isopentenyl)adenine + FAD + H2O
adenine + 3-methylbut-2-enal + FADH2
-
oxidative degradation of cytokinins
-
-
ir
N6-dimethylallyladenine + acceptor + H2O
adenine + 3-methylbut-2-enal + reduced acceptor
-
-
-
-
?
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
?
-
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
-
-
?
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
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
enzyme is strongly inhibited by flavin-protein oxidoreductase inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0011
N6-(2-isopentenyl)adenine
wild type enzyme, pH and temperature not specified in the publication
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
0.0041
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
additional information
additional information
kinetics, redox potential of electron acceptors
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
143.6
N6-(2-isopentenyl)adenine
pH 6.5, recombinant enzyme, with cofactor 2,3-dimethoxy-5-methyl-1,4-benzoquinone
129.8
N6-(2-isopentenyl)adenosine
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
activity in diverse tissues at pH 6.0 and pH 8.0, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
additional information
additional information
activity in diverse tissues at pH 6.0 and pH 8.0, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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 oxidase/dehydrogenase irreversibly degrades the plant hormones cytokinins and thereby participates in their homeostasis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CKX1_MAIZE
534
1
57229
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
enzyme amino acid sequence contains 5-8 putative glycosylation sites
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
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from yeast Yarrowia lipolytica by ammonium sulfate fractionation, gel filtration, and ion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in in Arabidopsis thaliana Ler suspension culture
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
expressed in in Arabidopsis thaliana Ler suspension culture
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Burch, L.R.; Horgan, R.
The purification of cytokinin oxidase from Zea mays kernels
Phytochemistry
28
1313-1319
1989
Triticum aestivum, Zea mays
-
McGaw, B.A.; Horgan, R.
Cytokinin catabolism and cytokinin oxidase
Phytochemistry
22
1103-1105
1983
Zea mays
-
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
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
-
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
-
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
-
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
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
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
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
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)
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
-
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
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
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
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
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
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
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
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
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)
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)
EXTERNAL LINKS (specific for EC-Number 1.5.99.12)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
