Literature summary for 1.2.1.80 extracted from

Sharma, A.; Shakeel, T.; Gupta, M.; Rajacharya, G.; Yazdani, S.
Biophysical and structural studies reveal marginal stability of a crucial hydrocarbon biosynthetic enzyme acyl ACP reductase (2021), Sci. Rep., 11, 12045 .

Search for more literature for 1.2.1.80

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Synechococcus elongatus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	2 mM used in assay conditions	Synechococcus elongatus

Organism

Organism	UniProt	Comment	Textmining
Synechococcus elongatus	Q54765	-	-
Synechococcus elongatus PCC 7942	Q54765	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA resin column chromatography and Superdex 200 gel filtration	Synechococcus elongatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
palmitoyl-CoA + NADPH + H+	-	Synechococcus elongatus	hexadecanal + CoA + NADP+	-	?
palmitoyl-CoA + NADPH + H+	-	Synechococcus elongatus PCC 7942	hexadecanal + CoA + NADP+	-	?

Subunits

Subunits	Comment	Organism
?	x * 38000, SDS-PAGE	Synechococcus elongatus
?	x * 40297, calculated from amino acid sequence	Synechococcus elongatus

Synonyms

Synonyms	Comment	Organism
AAR	-	Synechococcus elongatus
acyl-ACP reductase	-	Synechococcus elongatus
acyl-acyl carrier protein reductase	-	Synechococcus elongatus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
42.8	-	melting temperature	Synechococcus elongatus

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Synechococcus elongatus

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Release 2023.1 (January 2023)