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Literature summary for 4.1.2.17 extracted from

  • Garrabou, X.; Calveras, J.; Joglar, J.; Parella, T.; Bujons, J.; Clapes, P.
    Highly efficient aldol additions of DHA and DHAP to N-Cbz-amino aldehydes catalyzed by L-rhamnulose-1-phosphate and L-fuculose-1-phosphate aldolases in aqueous borate buffer (2011), Org. Biomol. Chem., 9, 8430-8436.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
F131A mutant with improved catalyti activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information for FucA catalysis, the rate of the aldol addition reaction of dihydroxyaceone phosphate to N-Cbz-amino aldehydes in borate is between 2 to 10 times faster than that inTEA buffer. Moreover, the yields of aldol adduct improve between 1.5 to 4-fold for both FucA wild-type and the F131A mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate + N-Cbz-(2R)-2-amino-3-methylbutanal wild-type 65% aldol adduct formed, mutant F131A, 76% aldol adduct formed Escherichia coli N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
-
?
dihydroxyacetone phosphate + N-Cbz-(2R)-2-amino-4-methylpentanal
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Escherichia coli N-Cbz-5-amino-1,3,4-trihydroxy-7-methyloctan-2-one
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-amino-3-methylbutanal wild-type 48% aldol adduct formed, mutant F131A, 60% aldol adduct formed Escherichia coli N-Cbz-5-amino-1,3,4-trihydroxyoctan-2-one
-
?
dihydroxyacetone phosphate + N-Cbz-(2S)-2-aminopropanal wild-type 65% aldol adduct formed, mutant F131A, 64% aldol adduct formed Escherichia coli N-Cbz-5-amino-1,3,4-trihydroxyhexan-2-one
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?
dihydroxyacetone phosphate + N-Cbz-aminoacetaldehyde wild-type 63% aldol adduct formed, mutant F131A, 50% aldol adduct formed Escherichia coli N-Cbz-5-amino-1,3,4-trihydroxypentan-2-one
-
?