EC Explorer

[browse EC tree] - [search]

EC 1.17.99.11 Details

show Brenda entry

EC number

1.17.99.11

Accepted name

3-oxo-Δ¹-steroid hydratase/dehydrogenase

Reaction

a 3-oxo-Δ¹-steroid + H₂O + acceptor = a steroid 1,3-dione + reduced acceptor (overall reaction);;(1a) a 3-oxo-Δ¹-steroid + H₂O = a 1-hydroxy-3-oxo-steroid;;(1b) a 1-hydroxy-3-oxo-steroid + acceptor = a steroid 1,3-dione + reduced acceptor

Other name(s)

atcABC (gene names)

Systematic name

3-oxo-Δ¹-steroid:acceptor 1-oxidoreductase

Comment

A molybdenum enzyme. The enzyme, characterized from the bacterium Steroidobacter denitrificans, is involved in the anaetrobic degradation of steroids. It is specific to 3-oxo-Δ¹-steroids such as androsta-1-ene-3,17-dione and Δ¹-dihydrotestosterone and does not act on 3-oxo-Δ⁴-steroids.

History

created 2020

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.2.1 glycerolphosphate dehydrogenase

1.1.2.2 mannitol dehydrogenase (cytochrome)

1.1.2.3 L-lactate dehydrogenase (cytochrome)

1.1.2.4 D-lactate dehydrogenase (cytochrome)

1.1.2.5 D-lactate dehydrogenase (cytochrome c-553)

1.1.2.6 polyvinyl alcohol dehydrogenase (cytochrome)

1.1.2.7 methanol dehydrogenase (cytochrome c)

1.1.2.8 alcohol dehydrogenase (cytochrome c)

1.1.2.9 1-butanol dehydrogenase (cytochrome c)

1.1.2.10 lanthanide-dependent methanol dehydrogenase

1.1.2.11 glucoside 3-dehydrogenase (cytochrome c)

1.1.3 With oxygen as acceptor

1.1.3.1 created 1961, deleted 1984

1.1.3.2 L-lactate oxidase

1.1.3.3 malate oxidase

1.1.3.4 glucose oxidase

1.1.3.5 hexose oxidase

1.1.3.6 cholesterol oxidase

1.1.3.7 aryl-alcohol oxidase

1.1.3.8 L-gulonolactone oxidase

1.1.3.9 galactose oxidase

1.1.3.10 pyranose oxidase

1.1.3.11 L-sorbose oxidase

1.1.3.12 pyridoxine 4-oxidase

1.1.3.13 alcohol oxidase

1.1.3.14 catechol oxidase (dimerizing)

1.1.3.15 (S)-2-hydroxy-acid oxidase

1.1.3.16 ecdysone oxidase

1.1.3.17 choline oxidase

1.1.3.18 secondary-alcohol oxidase

1.1.3.19 4-hydroxymandelate oxidase (decarboxylating)

1.1.3.20 long-chain-alcohol oxidase

1.1.3.21 glycerol-3-phosphate oxidase

1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004

1.1.3.23 thiamine oxidase

1.1.3.24 L-galactonolactone oxidase

1.1.3.25 created 1986, deleted 2005

1.1.3.26 created 1989, deleted 2002

1.1.3.27 hydroxyphytanate oxidase

1.1.3.28 nucleoside oxidase

1.1.3.29 N-acylhexosamine oxidase

1.1.3.30 polyvinyl-alcohol oxidase

1.1.3.31 created 1992, deleted 2003

1.1.3.32 created 1999, deleted 2002

1.1.3.33 created 1999, deleted 2002

1.1.3.34 created 1999, deleted 2002

1.1.3.35 created 1999, deleted 2002

1.1.3.36 created 1999, deleted 2002

1.1.3.37 D-arabinono-1,4-lactone oxidase

1.1.3.38 vanillyl-alcohol oxidase

1.1.3.39 nucleoside oxidase (H₂O₂-forming)

1.1.3.40 D-mannitol oxidase

1.1.3.41 alditol oxidase

1.1.3.42 prosolanapyrone-II oxidase

1.1.3.43 paromamine 6′-oxidase

1.1.3.44 6′′′-hydroxyneomycin C oxidase

1.1.3.45 aclacinomycin-N oxidase

1.1.3.46 4-hydroxymandelate oxidase

1.1.3.47 5-(hydroxymethyl)furfural oxidase

1.1.3.48 3-deoxy-α-D-manno-octulosonate 8-oxidase

1.1.3.49 (R)-mandelonitrile oxidase

1.1.3.50 C-glycoside oxidase

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

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

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.5 With a quinone or similar compound as acceptor

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.99 With unknown physiological acceptors

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

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.17.99.1 4-methylphenol dehydrogenase (hydroxylating)

1.17.99.2 ethylbenzene hydroxylase

1.17.99.3 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase

1.17.99.4 uracil/thymine dehydrogenase

1.17.99.5 bile-acid 7α-dehydroxylase

1.17.99.6 epoxyqueuosine reductase

1.17.99.7 formate dehydrogenase (acceptor)

1.17.99.8 limonene dehydrogenase

1.17.99.9 heme a synthase

1.17.99.10 steroid C-25 hydroxylase

1.17.99.11 3-oxo-Δ¹-steroid hydratase/dehydrogenase

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

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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)