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Literature summary extracted from

  • Athenstaedt, K.; Daum, G.
    1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles (2000), J. Biol. Chem., 275, 235-240.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.101 expression in Escherichia coli, YIL124w is the structural gene of the enzyme Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.101 33000
-
 lipid particles from wild type, systematic amino acid sequence analysis by mass spectrometry Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.101 acyldihydroxyacetone phosphate + NADPH Saccharomyces cerevisiae reaction in non-ether lipids biosynthesis 1-acyl-sn-glycerol 3-phosphate + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.101 Saccharomyces cerevisiae
-
 wild-type strain
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.101 acyldihydroxyacetone phosphate + NADPH
-
 Saccharomyces cerevisiae 1-acyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 acyldihydroxyacetone phosphate + NADPH reaction in non-ether lipids biosynthesis Saccharomyces cerevisiae 1-acyl-sn-glycerol 3-phosphate + NADP+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.101 NADPH specific for NADPH Saccharomyces cerevisiae
1.1.1.101 NADPH hydrogen from B-side of nicotinamide ring is transferred to reduce keto substrates Saccharomyces cerevisiae