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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.3.1.30 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]

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.30 Glycine max Q5MYA1
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.3.1.30 SAT1
-
 Glycine max
2.3.1.30 serine acetyltransferase
-
 Glycine max

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.30 22
-
 assay at room temperature Glycine max

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.30 7.3
-
 assay at Glycine max

General Information

EC Number General Information Comment Organism
2.3.1.30 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
2.3.1.30 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