Literature summary for 2.3.1.30 extracted from

Yi, H.; Dey, S.; Kumaran, S.; Lee, S.G.; Krishnan, H.B.; Jez, J.M.
Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone (2013), J. Biol. Chem., 288, 36463-36472.

Cloned(Commentary)

Cloned (Comment)	Organism
gene SAT1, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Glycine max

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme in apoform and complexed with L-serine and CoA, hanging drop vapor diffusion method, mixing of 0.005 ml of 10-20 mg/ml protein in 10 mM Tris, pH 8.0, 50 mM NaCl, and 5 mM 2-mercaptoethanol with 0.005 ml of reservoir solution, containing 1.8 M ammonium phosphate, 100 mM imidazole, pH 8.0, and equilibration ver 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.7-3.0 A resolution, method optimization	Glycine max

Crystallization (Comment)

Organism

purified enzyme in apoform and complexed with L-serine and CoA, hanging drop vapor diffusion method, mixing of 0.005 ml of 10-20 mg/ml protein in 10 mM Tris, pH 8.0, 50 mM NaCl, and 5 mM 2-mercaptoethanol with 0.005 ml of reservoir solution, containing 1.8 M ammonium phosphate, 100 mM imidazole, pH 8.0, and equilibration ver 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.7-3.0 A resolution, method optimization

Glycine max

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	steady-state kinetics	Glycine max

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + L-serine	Glycine max	-	CoA + O-acetyl-L-serine	-	?

Organism

Organism	UniProt	Comment	Textmining
Glycine max	Q5MYA1	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography	Glycine max

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + L-serine	-	Glycine max	CoA + O-acetyl-L-serine	-	?
additional information	ligand binding structures, overview	Glycine max	?	-	?

Synonyms

Synonyms	Comment	Organism
SAT1	-	Glycine max
serine acetyltransferase	-	Glycine max

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Glycine max

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.3	-	assay at	Glycine max

General Information

General Information	Comment	Organism
metabolism	serine acetyltransferase (SAT) catalyzes the limiting reaction in plant and microbial biosynthesis of cysteine. In addition to its enzymatic function, serine acetyltransferase forms a macromolecular complex with O-acetylserine sulfhydrylase, EC 2.5.1.47. Formation of the cysteine regulatory complex (CRC) is a critical biochemical control feature in plant sulfur metabolism. A role for CRC formation as a molecular chaperone to maintain SAT activity in response to an environmental stress, e.g. cold, is possible for the multienzyme complex in plants	Glycine max
additional information	enzyme residues His169 and Asp154 form a catalytic dyad for general base catalysis, and His189 may stabilize the oxyanion reaction intermediate. Glu177 helps to position Arg203 and His204 and the beta1c-beta2c loop for serine binding. A similar role for ionic interactions formed by Lys230 is required for CoA binding. Arg253 is important for the enhanced catalytic efficiency of SAT in the cysteine regulatory complex and suggest that movement of the residue may stabilize CoA binding in the macromolecular complex	Glycine max