Literature summary for 2.3.1.85 extracted from

Yu, X.; Liu, T.; Zhu, F.; Khosla, C.
In vitro reconstitution and steady-state analysis of the fatty acid synthase from Escherichia coli (2011), Proc. Natl. Acad. Sci. USA, 108, 18643-18648.

Cloned(Commentary)

Cloned (Comment)	Organism
individual overexpression of all components of fatty acid synthase in Escherichia coli	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
S36T	mutant in acyl carrier protein, mutant is incapable of undergoing phosphopantetheinylation. The S36T mutant is a weaker inhibitor of the fatty acid synthase than holo-acyl carrier protein, suggesting that the prostheticgroup of the acyl carrier protein contributes directly to its inhibitory characteristics at high concentrations	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	not inhibitory: NAD+ or NADP+ up to 5 mM	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
reconstitution of fatty acid synthase using purified protein components. When all ketosynthases are present at 1 microM, the maximum rate of free fatty acid synthesis of the fatty acid synthase exceeds 100 microM/min. The steady-state turnover frequency is not significantly inhibited at high concentrations of any substrate or cofactor. Fatty acid synthase activity is saturated with respect to most individual protein components when their concentrations exceeded 1 microM. The exceptions are protein components FabI and FabZ, which increase fatty acid synthase activity up to concentrations of 10 microM, FabH and FabF, which decrease fatty acid synthase activity at concentrations higher than 1 microM, and holo-acyl carrier protein and TesA, which give maximum fatty acid synthase activity at 30 microM concentrations	Escherichia coli

Renatured (Comment)

Organism

reconstitution of fatty acid synthase using purified protein components. When all ketosynthases are present at 1 microM, the maximum rate of free fatty acid synthesis of the fatty acid synthase exceeds 100 microM/min. The steady-state turnover frequency is not significantly inhibited at high concentrations of any substrate or cofactor. Fatty acid synthase activity is saturated with respect to most individual protein components when their concentrations exceeded 1 microM. The exceptions are protein components FabI and FabZ, which increase fatty acid synthase activity up to concentrations of 10 microM, FabH and FabF, which decrease fatty acid synthase activity at concentrations higher than 1 microM, and holo-acyl carrier protein and TesA, which give maximum fatty acid synthase activity at 30 microM concentrations

Escherichia coli