EC Explorer

[browse EC tree] - [search]

EC 1.1.1.313 Details

show Brenda entry

EC number

1.1.1.313

Accepted name

sulfoacetaldehyde reductase (NADPH)

Reaction

isethionate + NADP⁺ = 2-sulfoacetaldehyde + NADPH + H⁺

Other name(s)

isfD (gene name)

Systematic name

isethionate:NADP⁺ oxidoreductase

Comment

Catalyses the reaction only in the opposite direction. Involved in taurine degradation. The bacterium Chromohalobacter salexigens strain DSM 3043 possesses two enzymes that catalyse this reaction, a constitutive enzyme (encoded by isfD2) and an inducible enzyme (encoded by isfD). The latter is induced by taurine, and is responsible for most of the activity observed in taurine-grown cells. cf. EC 1.1.1.433, sulfoacetaldehyde reductase (NADH).

History

created 2011, modified 2022

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

1.1.3 With oxygen as acceptor

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

1.1.98.1 alcohol dehydrogenase (azurin)

1.1.98.2 glucose-6-phosphate dehydrogenase (coenzyme-F₄₂₀)

1.1.98.3 decaprenylphospho-β-D-ribofuranose 2-dehydrogenase

1.1.98.4 F₄₂₀H₂:quinone oxidoreductase

1.1.98.5 secondary-alcohol dehydrogenase (coenzyme-F₄₂₀)

1.1.98.6 ribonucleoside-triphosphate reductase (formate)

1.1.98.7 serine-type anaerobic sulfatase-maturating enzyme

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

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.10.1 With NAD⁺ or NADP⁺ as acceptor

1.10.2 With a cytochrome as acceptor

1.10.3 With oxygen as acceptor

1.10.3.1 catechol oxidase

1.10.3.2 laccase

1.10.3.3 L-ascorbate oxidase

1.10.3.4 o-aminophenol oxidase

1.10.3.5 3-hydroxyanthranilate oxidase

1.10.3.6 rifamycin-B oxidase

1.10.3.7 created 1986, deleted 2002

1.10.3.8 created 1986, deleted 2002

1.10.3.9 photosystem II

1.10.3.10 ubiquinol oxidase (H⁺-transporting)

1.10.3.11 ubiquinol oxidase (non-electrogenic)

1.10.3.12 menaquinol oxidase (H⁺-transporting)

1.10.3.13 caldariellaquinol oxidase (H⁺-transporting)

1.10.3.14 ubiquinol oxidase (electrogenic, non H⁺-transporting)

1.10.3.15 grixazone synthase

1.10.3.16 dihydrophenazinedicarboxylate synthase

1.10.3.17 superoxide oxidase

1.10.5 With a quinone or related compound as acceptor

1.10.9 With a copper protein as acceptor

1.10.99 With unknown physiological acceptors

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

1.18 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)

4.1 Carbon-carbon lyases

4.2 Carbon-oxygen lyases

4.3 Carbon-nitrogen lyases

4.4 Carbon-sulfur lyases

4.5 Carbon-halide lyases

4.6 Phosphorus-oxygen lyases

4.7 carbon-phosphorus lyases

4.8 Nitrogen-oxygen lyases

4.98 ATP-independent chelatases

4.99 Other lyases

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)