1.1.1.B57: 1-tetralone reductase [NADPH]

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For detailed information about 1-tetralone reductase [NADPH], go to the full flat file.

Word Map on EC 1.1.1.B57

1.1.1.B57

glucose-repressible

derepression

isozyme

catabolite

cis-dominant

nad+-dependent

mobilis

zymomonas

nonfermentable

transposable

nidulans

trans-acting

sporulate

analysis

Reaction

Synonyms

ADHII, MGG_02252, PAE2687, PyAeADHII, T4HNR, tetrahydroxynaphthalene reductase

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.B57 1-tetralone reductase [NADPH]

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Results	in table
2	AA Sequence
2	Application
1	Cloned(Commentary)
2	Cofactor
1	Crystallization (Commentary)
6	General Information
1	General Stability
3	IC50 Value
4	Inhibitors
1	KM Value [mM]
1	Metals/Ions
2	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
10	Organism
1	Purification (Commentary)
3	Reaction
6	Reference
2	Specific Activity [micromol/min/mg]
18	Substrates and Products (Substrate)
4	Subunits
14	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.B57 - 1-tetralone reductase [NADPH]

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crystal structure of both wild-type and cobalt-substituted enzyme at 1.75 A and 2.20 A resolution, respectively. One metal ion per monomer is present only at the structural site. The co-crystal structure of the NADPH-bound form of the enzyme at 2.35 A resolution shows close structural conservation with horse ADH, despite the lack of a catalytic Zn2+. Modeling of 1-tetralone into the NADPH-bound structure suggests an arginine as a possible catalytic residue

Pyrobaculum aerophilum

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