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Literature summary extracted from

  • Fornarotto, M.; Xiao, L.; Hou, Y.; Koch, K.A.; Chang, E.; OMalley, R.M.; Black, T.A.; Cable, M.B.; Walker, S.S.
    Sphingolipid biosynthesis in pathogenic fungi: identification and characterization of the 3-ketosphinganine reductase activity of Candida albicans and Aspergillus fumigatus (2006), Biochim. Biophys. Acta, 1761, 52-63.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.102 gene ksr1, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain JM109(DE3) Candida albicans
1.1.1.102 gene ksrA, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain JM109(DE3) Aspergillus fumigatus
1.1.1.102 gene tsc10, expression of mutant tscDELTA38 in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.102 additional information construction of an enzyme-deficient mutant by gene replacement, the mutant produces lower levels of inositolphosphorylceramides Candida albicans
1.1.1.102 additional information construction of the deletion mutant TscDELTA38p Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.102 additional information
-
 additional information binding kinetics of substrate analogues with shorter chain lengths Candida albicans
1.1.1.102 0.009
-
 3-dehydrosphinganine pH 7.5, recombinant enzyme Candida albicans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.102 3-dehydrosphinganine + NADPH Aspergillus fumigatus
-
 sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH Saccharomyces cerevisiae the enzyme catalyzes an early step in the sphingolipid biosynthesis, overview sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH Candida albicans the enzyme is not essential for cell viability, but enzyme-deficient mutants produce lower levels of inositolphosphorylceramides sphinganine + NADP+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.102 Aspergillus fumigatus
-
 gene ksrA
-
1.1.1.102 Candida albicans
-
 gene ksr1
-
1.1.1.102 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.102 3-dehydrosphinganine + NADPH
-
 Saccharomyces cerevisiae sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH
-
 Aspergillus fumigatus sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH the enzyme catalyzes an early step in the sphingolipid biosynthesis, overview Saccharomyces cerevisiae sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH the enzyme is not essential for cell viability, but enzyme-deficient mutants produce lower levels of inositolphosphorylceramides Candida albicans sphinganine + NADP+
-
 ?
1.1.1.102 3-dehydrosphinganine + NADPH C18 substrate, molecular modeling of substrate binding, overview Candida albicans sphinganine + NADP+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.102 More molecular modeling of the enzyme with bound substrates, a significant portion of the aliphatic chain of 3-dehydrosphinganine protrudes from the enzyme, overview Candida albicans

Synonyms

EC Number Synonyms Comment Organism
1.1.1.102 3-ketosphinganine reductase
-
 Saccharomyces cerevisiae
1.1.1.102 3-ketosphinganine reductase
-
 Candida albicans
1.1.1.102 3-ketosphinganine reductase
-
 Aspergillus fumigatus
1.1.1.102 Ksr1p
-
 Candida albicans
1.1.1.102 KsrA
-
 Aspergillus fumigatus
1.1.1.102 More the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes Saccharomyces cerevisiae
1.1.1.102 More the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes Candida albicans
1.1.1.102 More the enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes Aspergillus fumigatus
1.1.1.102 TSC10
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.102 1.07
-
 3-dehydrosphinganine pH 7.5, recombinant enzyme Candida albicans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.102 7.5
-
 assay at Saccharomyces cerevisiae
1.1.1.102 7.5
-
 assay at Candida albicans
1.1.1.102 7.5
-
 assay at Aspergillus fumigatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.102 NADPH
-
 Saccharomyces cerevisiae
1.1.1.102 NADPH
-
 Candida albicans
1.1.1.102 NADPH
-
 Aspergillus fumigatus