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Literature summary for 2.3.1.15 extracted from

  • Hayman, M.W.; Fawcett, T.; Slabas, A.R.
    Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata) (2002), FEBS Lett., 514, 281-284.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminal truncated enzyme in Escherichia coli, overexpression of wild-type acyltransferase in tobacco Cucurbita moschata
overexpression in tobacco Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003 0.0034 acyl-ACP recombinant N-terminal truncated acyltransferase Cucurbita moschata

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-
Cucurbita moschata
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an acyl-CoA + sn-glycerol 3-phosphate = CoA + a 1-acyl-sn-glycerol 3-phosphate reaction proceeds via a compulsory-ordered ternary with acyl-ACP binding before glycerol 3-phosphate Cucurbita moschata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + sn-glycerol 3-phosphate very low activity with butanoyl-CoA and hexanoyl-CoA Cucurbita moschata CoA + 1-acyl-sn-glycerol 3-phosphate
-
?
acyl-[acyl-carrier protein] + sn-glycerol 3-phosphate
-
Cucurbita moschata acyl-carrier protein + 1-acyl-sn-glycerol 3-phosphate
-
?