Serine O-acetyltransferase

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serine O-acetyltransferase
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MetaCycmetabolic pathway
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In

enzymology, a serine O-acetyltransferase (EC 2.3.1.30) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + L-serine CoA + O-acetyl-L-serine

Thus, the two

O-acetyl-L-serine
.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:L-serine O-acetyltransferase. Other names in common use include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase. This enzyme participates in cysteine metabolism and sulfur metabolism.

Structural studies

As of late 2007, 7

structures have been solved for this class of enzymes, with PDB accession codes 1S80, 1SSM, 1SSQ, 1SST, 1T3D, 1Y7L, and 2ISQ
.

N terminal protein domain

SATase N terminal domain
The structure of the enzyme serine acetyltransferase- apoenzyme (truncated)
Identifiers
SymbolSATase_N
PfamPF06426
InterProIPR010493
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In

Importance of function

The N-terminal domain of the protein Serine acetyltransferase helps catalyse

transgenic plants. These transgenic plants would contain more essential sulphur amino acids meaning a healthier diet for humans and animals.[3]

Structure

The amino-terminal

acetyl transfer.[4] There are eight alpha helices that form the N-terminal domain.[4]

References