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EC 1.14.13.144 Details

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EC number

1.14.13.144

Accepted name

9β-pimara-7,15-diene oxidase

Reaction

9β-pimara-7,15-diene + 3 O₂ + 3 NADPH + 3 H⁺ = 9β-pimara-7,15-dien-19-oate + 3 NADP⁺ + 4 H₂O (overall reaction);;(1a) 9β-pimara-7,15-diene + O₂ + NADPH + H⁺ = 9β-pimara-7,15-dien-19-ol + NADP⁺ + H₂O;;(1b) 9β-pimara-7,15-dien-19-ol + O₂ + NADPH + H⁺ = 9β-pimara-7,15-dien-19-al + NADP⁺ + 2 H₂O;;(1c) 9β-pimara-7,15-dien-19-al + O₂ + NADPH + H⁺ = 9β-pimara-7,15-dien-19-oate + NADP⁺ + H₂O;;

Other name(s)

CYP99A3

Systematic name

9β-pimara-7,15-diene,NADPH:oxygen 19-oxidoreductase

Comment

Requires cytochrome P-450. A rice, Oryza sativa, enzyme involved in the phytoalexin momilactone biosynthesis. It also acts similarly on 9β-stemod-13(17)-ene.

History

created 2012, deleted 2018

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.3.1 With NAD⁺ or NADP⁺ as acceptor

1.3.2 With a cytochrome as acceptor

1.3.3 With oxygen as acceptor

1.3.4 With a disulfide as acceptor

1.3.5 With a quinone or related compound as acceptor

1.3.7 With an iron-sulfur protein as acceptor

1.3.8 With a flavin as acceptor

1.3.98 With other, known, physiological acceptors

1.3.99 With unknown physiological acceptors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.6.1 In phosphorus-containing anhydrides

3.6.1.1 inorganic diphosphatase

3.6.1.2 trimetaphosphatase

3.6.1.3 adenosinetriphosphatase

3.6.1.4 created 1961, deleted 1965

3.6.1.5 apyrase

3.6.1.6 nucleoside diphosphate phosphatase

3.6.1.7 acylphosphatase

3.6.1.8 ATP diphosphatase

3.6.1.9 nucleotide diphosphatase

3.6.1.10 endopolyphosphatase

3.6.1.11 exopolyphosphatase

3.6.1.12 dCTP diphosphatase

3.6.1.13 ADP-ribose diphosphatase

3.6.1.14 adenosine-tetraphosphatase

3.6.1.15 nucleoside-triphosphate phosphatase

3.6.1.16 CDP-glycerol diphosphatase

3.6.1.17 bis(5′-nucleosyl)-tetraphosphatase (asymmetrical)

3.6.1.18 FAD diphosphatase

3.6.1.19 nucleoside-triphosphate diphosphatase

3.6.1.20 5′-acylphosphoadenosine hydrolase

3.6.1.21 ADP-sugar diphosphatase

3.6.1.22 NAD⁺ diphosphatase

3.6.1.23 dUTP diphosphatase

3.6.1.24 nucleoside phosphoacylhydrolase

3.6.1.25 triphosphatase

3.6.1.26 CDP-diacylglycerol diphosphatase

3.6.1.27 undecaprenyl-diphosphate phosphatase

3.6.1.28 thiamine-triphosphatase

3.6.1.29 bis(5′-adenosyl)-triphosphatase

3.6.1.30 m⁷G(5′)pppN diphosphatase

3.6.1.31 phosphoribosyl-ATP diphosphatase

3.6.1.32 created 1984, deleted 2000

3.6.1.33 created 1984, deleted 2000

3.6.1.34 created 1984, deleted 2000

3.6.1.35 created 1984, deleted 2000

3.6.1.36 created 1984, deleted 2000

3.6.1.37 created 1984, deleted 2000

3.6.1.38 created 1984, deleted 2000

3.6.1.39 thymidine-triphosphatase

3.6.1.40 guanosine-5′-triphosphate,3′-diphosphate phosphatase

3.6.1.41 bis(5′-nucleosyl)-tetraphosphatase (symmetrical)

3.6.1.42 guanosine-diphosphatase

3.6.1.43 dolichyldiphosphatase

3.6.1.44 oligosaccharide-diphosphodolichol diphosphatase

3.6.1.45 UDP-sugar diphosphatase

3.6.1.46 created 2000, deleted 2003

3.6.1.47 created 2000, deleted 2003

3.6.1.48 created 2000, deleted 200

3.6.1.49 created 2000, deleted 2003

3.6.1.50 created 2000, deleted 2003

3.6.1.51 created 2000, deleted 2003

3.6.1.52 diphosphoinositol-polyphosphate diphosphatase

3.6.1.53 Mn²⁺-dependent ADP-ribose/CDP-alcohol diphosphatase

3.6.1.54 UDP-2,3-diacylglucosamine diphosphatase

3.6.1.55 8-oxo-dGTP diphosphatase

3.6.1.56 2-hydroxy-dATP diphosphatase

3.6.1.57 UDP-2,4-diacetamido-2,4,6-trideoxy-β-L-altropyranose hydrolase

3.6.1.58 8-oxo-dGDP phosphatase

3.6.1.59 5′-(N⁷-methyl 5′-triphosphoguanosine)-[mRNA] diphosphatase

3.6.1.60 diadenosine hexaphosphate hydrolase (AMP-forming)

3.6.1.61 diadenosine hexaphosphate hydrolase (ATP-forming)

3.6.1.62 5′-(N⁷-methylguanosine 5′-triphospho)-[mRNA] hydrolase

3.6.1.63 α-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

3.6.1.64 inosine diphosphate phosphatase

3.6.1.65 (d)CTP diphosphatase

3.6.1.66 XTP/dITP diphosphatase

3.6.1.67 dihydroneopterin triphosphate diphosphatase

3.6.1.68 geranyl diphosphate phosphohydrolase

3.6.1.69 8-oxo-(d)GTP phosphatase

3.6.1.70 guanosine-5′-diphospho-5′-[DNA] diphosphatase

3.6.1.71 adenosine-5′-diphospho-5′-[DNA] diphosphatase

3.6.1.72 DNA-3′-diphospho-5′-guanosine diphosphatase

3.6.1.73 inosine/xanthosine triphosphatase

3.6.1.74 mRNA 5′-phosphatase

3.6.1.75 diacylglycerol diphosphate phosphatase

3.6.2 In sulfonyl-containing anhydrides

3.6.3 Acting on acid anhydrides to catalyse transmembrane movement of substances

3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement

3.6.5 Acting on GTP to facilitate cellular and subcellular movement

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)