1.1.1.368: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

This is an abbreviated version!
For detailed information about 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, go to the full flat file.

Reaction

Synonyms

HAD, ThaADH

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.368 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

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Results	in table
221	AA Sequence
2	Cloned(Commentary)
2	Cofactor
2	Expression
3	General Information
1	Inhibitors
1	KM Value [mM]
2	Metals/Ions
2	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
2	Organism
7	Pathway
4	PDB ID
3	pH Optimum
1	pH Range
2	Purification (Commentary)
1	Reaction
2	Reference
1	Source Tissue
1	Specific Activity [micromol/min/mg]
6	Substrates and Products (Substrate)
2	Subunits
2	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Turnover Number [1/s]

General Information

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General Information on EC 1.1.1.368 - 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase

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evolution

Thauera aromatica

the enzyme belongs to the zinc-dependent alcohol dehydrogenases (ADHs)

741556

metabolism

Thauera aromatica

the enzyme is involved in the benzoate degradation pathway

741556

additional information

Thauera aromatica

ThaADH three-dimensional structure modeling overview. A bulky aromatic residue, that plays a crucial role in the definition of the substrate binding pockets of most ADHs, is replaced by a glycine residue in ThaADH. This structural difference leads to the formation of one large binding pocket instead of two smaller ones and consequently to a preference for cyclic diketones over linear bulky substrates

741556