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Information on EC 1.14.14.179 - brassinosteroid 6-oxygenase
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EC Tree
1.14.14.179 brassinosteroid 6-oxygenaseIUBMB Comments
This cytochrome P-450 (heme thiolate) plant enzyme catalyses the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group. Substrates include 6-deoxocastasterone, 6-deoxotyphasterol, 3-dehydro-6-deoxoteasterone, and 6-deoxoteasterone. The CYP85A2 isozyme of Arabidopsis thaliana (but not the CYP85A1 isozyme) also catalyses the activity of EC 1.14.14.180, brassinolide synthase.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
2
=
+
3
+
2
6-deoxocastasterone
+
2
+
2
[reduced NADPHhemoprotein reductase]
=
+
3
+
2
[oxidized NADPHhemoprotein reductase]
Synonyms
dwarf, cyp85a2, cyp85a1, cyp85, br6ox2, br6ox1, cyp85a3, brassinosteroid-deficient dwarf1, atbr6ox, brassinosteroid-dependent 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
brassinosteroid 6-oxidase
-
-
-
-
Brd1
CYP85A1
CYP85A2
CYP85A3
dwarf
CYP85A1
-
-
-
-
CYP85A2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6-deoxocastasterone + 2 O2 + 2 [reduced NADPHhemoprotein reductase] = castasterone + 3 H2O + 2 [oxidized NADPHhemoprotein reductase]
overall reaction
-
-
-
6-deoxocastasterone + O2 + [reduced NADPHhemoprotein reductase] = 6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPHhemoprotein reductase]
(1a)
-
-
-
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPHhemoprotein reductase] = castasterone + 2 H2O + [oxidized NADPHhemoprotein reductase]
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
6-deoxocastasterone,NADPH-hemoprotein reductase:oxygen 6-oxidoreductase (castasterone-forming)
This cytochrome P-450 (heme thiolate) plant enzyme catalyses the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group. Substrates include 6-deoxocastasterone, 6-deoxotyphasterol, 3-dehydro-6-deoxoteasterone, and 6-deoxoteasterone. The CYP85A2 isozyme of Arabidopsis thaliana (but not the CYP85A1 isozyme) also catalyses the activity of EC 1.14.14.180, brassinolide synthase.
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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
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
additional information
?
-
no substrates: campestanol , 6-deoxocathasterone
-
-
-
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
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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
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
3-dehydro-6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
3-dehydroteasterone+ H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
castasterone + 3 H2O + 2 [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
6alpha-hydroxy-6-deoxocastasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxoteasterone + O2 + [reduced NADPH-hemoprotein reductase]
teasterone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6-deoxotyphasterol + O2 + [reduced NADPH-hemoprotein reductase]
typhasterol + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
6alpha-hydroxy-6-deoxocastasterone + O2 + [reduced NADPH-hemoprotein reductase]
castasterone + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, possesses brassinosteroid C-6 oxidase and brassinolide synthase activity, reactions of ECs 1.14.14.179 and 1.14.14.180
UniProt
brenda
cf. EC 1.14.14.180, bifunctional brassinosteroid 6-oxygenase and brassinolide synthase
UniProt
brenda
cf. EC 1.14.14.180, bifunctional brassinosteroid 6-oxygenase and brassinolide synthase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
CYP85A1 mRNA is localized in the female gametophyte. Within the ovule the corresponding protein is mostly active in gametophytic cells
brenda
additional information
gene is expressed at a low level in all of the examined tissues
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
in a phylogenetic tree, tomato CYP85A3 is placed on the same branch as the CYP85A family of tomato, Arabidopsis, and rice, and is closest to tomato CYP85A1
metabolism
physiological function
metabolism
enzyme catalyzes the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group
metabolism
enzyme catalyzes the C-6 hydoxylation of several brassinosteroid biosynthesis intermediates, and the further oxidation of the hydroxyl group to an oxo group
physiological function
a mutant defective in BRD1 has very short leaf sheaths, has short, curled, and frizzled leaf blades, has few tillers and is sterile under normal growth conditions. Exogenously supplied brassinolide considerably restores the normal phenotype. Under darkness, the mutant shows constitutive photomorphogenesis
physiological function
BRD1 mutants show defects in the elongation of the stem and leaves, primarily owing to a failure in the organization and polar elongation of the leaf and stem cells
physiological function
Brd1 mutation lil-1 causes alterations in the root gravitropic response, leaf epidermal cell density, epicuticular wax deposition and seedling adaptation to water scarcity conditions
physiological function
CYP85A1 mutants do not show any obvious morphological phenotype during vegetative or floral development. Mutants defective in the activity of CYP85A1 exhibit a semi-sterile phenotype. Of heterozygous cyp85a1/+ individuals, close to 50% of female gametophytes are arrested before the first nuclear mitotic division of the haploid functional megaspore
physiological function
CYP85A2 additionally catalyzes the lactonization reactions of castasterone and also teasterone and typhasterol. A Pichia pastoris transformant that synchronously expresses Arabidopsis thaliana P450 reductase gene ATR1 and P450 gene CYP85A2 converts teasterone and typhasterol to 7-oxateasterone and 7-oxatyphasterol, respectively
physiological function
enzyme is a cytochrome P450 that mediates Baeyer-Villiger oxidation in plants. Castasterone is a bioactive brassinosteroid that controls the overall growth and development of Arabidopsis plants. Mutant studies also revealed that brassinolide may not always be necessary for normal growth and development but Arabidopsis plants acquire great benefit in terms of growth and development in the presence of brassinolide
physiological function
-
mutants plants lacking Brd1 activity have essentially no internode elongation and exhibit no etiolation response when germinated in the dark. The phenotypes can be rescued by exogenous application of brassinolide. The mutant plants also display alterations in leaf and floral morphology. The meristem is not altered in size but there are differences in the cellular structure of several tissues
physiological function
overexpression in seeds increases the levels of castasterone and brassinolide in seeds. Compared to the wild type, the overexpressing strains produces substantially larger seeds with a high concentration of nutrients due to an enhancement in brassinosteroids signaling. Additionally, it exhibits superior seed germination, seedling and rosette plant growth, and flower and silique formation
physiological function
-
Picea abies possesses functional CYP85A1 and receptor BRL1 but not CYP85A2 or BRI1, resulting in weak brassinosteroids signaling, and both CYP85A and BRL1 are abundantly expressed. Neither brassinosteroids treatment of Picea abies seedlings nor expression of BRL1 in the Arabidopsis Atbri1 mutant promote plant height
physiological function
-
poplar plants overexpressing CYP85A3 produce thicker G-layer with higher cellulose proportion, and accumulate more transcriptional factor BZR1 protein in the xylem of tension wood than the wild-type plants. Expression of most tension wood-associated cellulose synthases is also up-regulated in the xylem of tension wood in transgenic plants
physiological function
seeds of transgenic Brachypodium distachyon expressing CYP85A2 synthesize castasterone. In comparison with wild-type B. distachyon, the transgenic plants show better growth and development during the vegetative growing stage. The flowers of the transgenic plants are remarkably larger, resulting in increments in the number, size, and height of seeds. The total starch, protein, and lipid contents in transgenic plants are higher than those in wild-type plants
physiological function
there are campestanol-dependent and campestanol-independent pathways in Brachypodium distachyon that synthesize 24-methylated brassinosteroids. Brassinolide is not identified
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
farnesylation
both the secretory signal at the N-terminus and the farnesylation motif at the C-terminus are required for functionality of CYP85A2
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the C-terminal CaaX motif of CYP85A2 can still target CYPA85A2 in the absence of an intact N-terminal secretory signal to the endoplasmic reticulum. In the absence of both the CaaX motif and the secretory signal, CYP85A2 is not targeted to the membranes and becomes unstable
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in yeast
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP85A1 is abundantly expressed in wild-type, but not in sporocyteless ovules lacking a female gametophyte
expression is negatively regulated by brassinolide treatment
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
overexpression in seeds increases the levels of castasterone and brassinolide in seeds. Compared to the wild type, the overexpressing strains produces substantially larger seeds with a high concentration of nutrients due to an enhancement in brassinosteroids signaling. Additionally, it exhibits superior seed germination, seedling and rosette plant growth, and flower and silique formation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Castorina, G.; Persico, M.; Zilio, M.; Sangiorgio, S.; Carabelli, L.; Consonni, G.
The maize lilliputian1 (lil1) gene, encoding a brassinosteroid cytochrome P450 C-6 oxidase, is involved in plant growth and drought response
Ann. Bot.
122
227-238
2018
Zea mays (A0A317YAX4), Zea mays
brenda
Katsumata, T.; Hasegawa, A.; Fujiwara, T.; Komatsu, T.; Notomi, M.; Abe, H.; Natsume, M.; Kawaide, H.
Arabidopsis CYP85A2 catalyzes lactonization reactions in the biosynthesis of 2-deoxy-7-oxalactone brassinosteroids
Biosci. Biotechnol. Biochem.
72
2110-2117
2008
Arabidopsis thaliana (Q940V4)
brenda
Jin, Y.; Yu, C.; Jiang, C.; Guo, X.; Li, B.; Wang, C.; Kong, F.; Zhang, H.; Wang, H.
PtiCYP85A3, a BR C-6 oxidase gene, plays a critical role in brassinosteroid-mediated tension wood formation in poplar
Front. Plant Sci.
11
468
2020
Populus trichocarpa
brenda
Roh, J.; Moon, J.; Lee, Y.; Park, C.; Kim, S.
Seed-specific expression of Arabidopsis AtCYP85A2 produces biologically active brassinosteroids such as castasterone and brassinolide to improve grain yield and quality in seeds of Brachypodium distachyon
Front. Plant Sci.
12
639508
2021
Arabidopsis thaliana (Q940V4)
brenda
Roh, J.; Moon, J.; Youn, J.H.; Seo, C.; Park, Y.J.; Kim, S.K.
Establishment of biosynthetic pathways to generate castasterone as the biologically active brassinosteroid in Brachypodium distachyon
J. Agric. Food Chem.
68
3912-3923
2020
Brachypodium distachyon (I1GQE7), Brachypodium distachyon
brenda
Nomura, T.; Kushiro, T.; Yokota, T.; Kamiya, Y.; Bishop, G.J.; Yamaguchi, S.
The last reaction producing brassinolide is catalyzed by cytochrome P-450s, CYP85A3 in tomato and CYP85A2 in Arabidopsis
J. Biol. Chem.
280
17873-17879
2005
Solanum lycopersicum (Q50LE0), Solanum lycopersicum
brenda
Wang, L.; Liu, J.; Shen, Y.; Pu, R.; Hou, M.; Wei, Q.; Zhang, X.; Li, G.; Ren, H.; Wu, G.
Brassinosteroids synthesised by CYP85A/A1 but not CYP85A2 function via a BRI1-like receptor but not via BRI1 in Picea abies
J. Exp. Bot.
72
1748-1763
2021
Picea abies
brenda
Yeon, M.; Park, C.; Lee, Y.; Roh, J.; Kim, S.
Seed-specifically overexpressed Arabidopsis cytochrome P450 85A2 promotes vegetative and reproductive growth and development of Arabidopsis thaliana
J. Plant Biol.
65
75-86
2022
Arabidopsis thaliana (Q940V4)
-
brenda
Kim, T.W.; Hwang, J.Y.; Kim, Y.S.; Joo, S.H.; Chang, S.C.; Lee, J.S.; Takatsuto, S.; Kim, S.K.
Arabidopsis CYP85A2, a cytochrome P450, mediates the Baeyer-Villiger oxidation of castasterone to brassinolide in brassinosteroid biosynthesis
Plant Cell
17
2397-2412
2005
Arabidopsis thaliana (Q940V4), Arabidopsis thaliana
brenda
Hong, Z.; Ueguchi-Tanaka, M.; Shimizu-Sato, S.; Inukai, Y.; Fujioka, S.; Shimada, Y.; Takatsuto, S.; Agetsuma, M.; Yoshida, S.; Watanabe, Y.; Uozu, S.; Kitano, H.; Ashikari, M.; Matsuoka, M.
Loss-of-function of a rice brassinosteroid biosynthetic enzyme, C-6 oxidase, prevents the organized arrangement and polar elongation of cells in the leaves and stem
Plant J.
32
495-508
2002
Oryza sativa Japonica Group (Q8GSQ1)
brenda
Shimada, Y.; Fujioka, S.; Miyauchi, N.; Kushiro, M.; Takatsuto, S.; Nomura, T.; Yokota, T.; Kamiya, Y.; Bishop, G.; Yoshida, S.
Brassinosteroid-6-oxidases from Arabidopsis and tomato catalyze multiple C-6 oxidations in brassinosteroid biosynthesis1
Plant Physiol.
126
770-779
2001
Solanum lycopersicum (Q43147), Solanum lycopersicum, Arabidopsis thaliana (Q9FMA5)
brenda
Mori, M.; Nomura, T.; Ooka, H.; Ishizaka, M.; Yokota, T.; Sugimoto, K.; Okabe, K.; Kajiwara, H.; Satoh, K.; Yamamoto, K.; Hirochika, H.; Kikuchi, S.
Isolation and characterization of a rice dwarf mutant with a defect in brassinosteroid biosynthesis
Plant Physiol.
130
1152-1161
2002
Oryza sativa Japonica Group (Q8GSQ1)
brenda
Jamshed, M.; Liang, S.; M N Hickerson, N.; Samuel, M.A.
Farnesylation-mediated subcellular localization is required for CYP85A2 function
Plant Signal. Behav.
12
e1382795
2017
Arabidopsis thaliana (Q940V4)
brenda
Perez-Espana, V.H.; Sanchez-Leon, N.; Vielle-Calzada, J.P.
CYP85A1 is required for the initiation of female gametogenesis in Arabidopsis thaliana
Plant Signal. Behav.
6
321-326
2011
Arabidopsis thaliana (Q9FMA5), Arabidopsis thaliana
brenda
Makarevitch, I.; Thompson, A.; Muehlbauer, G.J.; Springer, N.M.
Brd1 gene in maize encodes a brassinosteroid C-6 oxidase
PLoS ONE
7
e30798
2012
Zea mays
brenda
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