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Literature summary extracted from

  • Racenis, P.V.; Lai, J.L.; Das, A.K.; Mullick, P.C.; Hajra, A.K.; Greenberg, M.L.
    The acyl dihydroxyacetone phosphate pathway enzymes for glycerolipid biosynthesis are present in the yeast Saccharomyces cerevisiae (1992), J. Bacteriol., 174, 5704-5710.
No PubMed abstract available

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.101 divalent cations i.e. Cu2+, Co2+, Ca2+, Mg2+, Mn2+, Ni2+, Zn2+, strong inhibition Saccharomyces cerevisiae
1.1.1.101 EDTA weak inhibition Saccharomyces cerevisiae
1.1.1.101 F- weak inhibition Saccharomyces cerevisiae
1.1.1.101 N-ethylmaleimide strong inhibitor Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.101 0.015
-
 NADPH cosubstrate hexadecyldihydroxyacetone phosphate Saccharomyces cerevisiae
1.1.1.101 0.02
-
 NADPH
-
 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 acyldihydroxyacetone phosphate pathway 1-acyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 acyldihydroxyacetone phosphate + NADPH Saccharomyces cerevisiae reaction in non-ether lipids biosynthesis 1-acyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 alkyldihydroxyacetone phosphate + NADPH + H+ Saccharomyces cerevisiae acyldihydroxyacetone phosphate pathway 1-alkyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 alkyldihydroxyacetone phosphate + NADPH + H+ Saccharomyces cerevisiae reaction in ether lipids biosynthesis 1-alkyl-sn-glycerol 3-phosphate + NADP+
-
 ?

Organism

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

Storage Stability

EC Number Storage Stability Organism
1.1.1.101 -20°C, membrane fraction stable Saccharomyces cerevisiae
1.1.1.101 -80°C, membrane fraction stable Saccharomyces cerevisiae

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 acyldihydroxyacetone phosphate pathway 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+
-
 ?
1.1.1.101 alkyldihydroxyacetone phosphate + NADPH + H+
-
 Saccharomyces cerevisiae 1-alkyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 alkyldihydroxyacetone phosphate + NADPH + H+ acyldihydroxyacetone phosphate pathway Saccharomyces cerevisiae 1-alkyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 alkyldihydroxyacetone phosphate + NADPH + H+ reaction in ether lipids biosynthesis Saccharomyces cerevisiae 1-alkyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 hexadecyldihydroxyacetone phosphate + NADPH
-
 Saccharomyces cerevisiae 1-hexadecyl-sn-glycerol 3-phosphate + NADP+
-
 ?
1.1.1.101 palmitoylglycerone phosphate + NADPH i.e. palmitoyldihydroxyacetone phosphate Saccharomyces cerevisiae 1-palmitoylglycerol 3-phosphate + NADP+
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.101 40
-
-
 Saccharomyces cerevisiae

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.101 28 43 about half-maximal activity at 28°C and 43°C Saccharomyces cerevisiae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.101 30
-
 10 min stable below Saccharomyces cerevisiae
1.1.1.101 45
-
 t1/2: 10 min Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.101 6.7 7.2 broad optimum Saccharomyces cerevisiae

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