1.1.1.373: sulfolactaldehyde 3-reductase

This is an abbreviated version!
For detailed information about sulfolactaldehyde 3-reductase, go to the full flat file.

Reaction

Synonyms

3-sulfolactaldehyde reductase, 3-sulpholactaldehyde reductase, NADH-dependent SLA reductase, SLA reductase, sulfolactaldehyde reductase, yihU

ECTree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.373 sulfolactaldehyde 3-reductase

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Results	in table
994	AA Sequence
2	Cloned(Commentary)
6	Cofactor
2	Crystallization (Commentary)
3	General Information
4	IC50 Value
5	Inhibitors
16	kcat/KM [mM/s]
2	Ki Value [mM]
17	KM Value [mM]
1	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
3	Organism
3	Pathway
12	PDB ID
6	Protein Variants
1	Purification (Commentary)
2	Reaction
3	Reference
2	Source Tissue
7	Substrates and Products (Substrate)
2	Subunits
11	Synonyms
1	Systematic Name
16	Turnover Number [1/s]

Subunits

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Subunits on EC 1.1.1.373 - sulfolactaldehyde 3-reductase

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homotetramer

Escherichia coli

P0A9V8

4 * 30000, calculated from amino acid sequence

762529

tetramer

Escherichia coli

P0A9V8

YihU forms a dimer of intimate homodimer pairs. The enzyme exuísts as a tetramer in crystal and in solution. Within the asymmetric unit, each protomer adopts a two-domain architecture containing an N-terminal nucleotide-binding domain (residues 1-164) and a C-terminal helical bundle (residues 165-294) both connected by the long interdomain helix alpha8. The N-terminal domain is composed of a classical alpha/beta Rossmann fold (composed of an extended sheet formed by beta1-6, flanked by alpha1-5 in a three-layered sandwich) appended with an additional beta-alpha-beta motif containing beta7-9 and alpha6. Four interfaces are present within the subunits of the YihU tetramer. Detailed structure analysis, overview

762529