Literature summary for 2.5.1.47 extracted from

Wang, T.; Leyh, T.S.
Three-stage assembly of the cysteine synthase complex from Escherichia coli (2012), J. Biol. Chem., 287, 4360-4367.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Synonyms

Synonyms	Comment	Organism
CSC	-	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	cysteine synthase complex CSC is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis: serine O-acetyltransferase, EC 2.3.1.30, which produces O-acetyl-L-serine, and O-acetyl-L-serine sulfhydrylase, EC 2.5.1.47, which converts it to cysteine. The system exhibits a contact-induced inactivation of half of each biomolecule, and exhibits a mechanism in which serine O-acetyltransferase interacts with O-acetyl-L-serine sulfhydrylase in a nonallosteric interaction involving its C-terminus. This early docking event appears to fasten the proteins in close proximity. The complex passes through at least three stable conformations in achieving its most stable configuration. Binding of a serine O-acetyltransferase C-terminal peptide is monophasic, and binding at one O-acetyl-L-serine sulfhydrylase active site does not prevent, or otherwise influence, binding at the second. The rate constants governing the first phase of the serine O-acetyltransferase binding reaction are remarkably similar to those for the binding of peptide, suggesting that early docking of serine O-acetyltransferase occurs primarily through the its C-terminus. The inability of the peptide to either induce isomerization or close the distal site suggests that serine O-acetyltransferase structure beyond its C-terminus is required to engage in isomerization and that closure of the unoccupied O-acetyl-L-serine sulfhydrylase active site may be coupled to the one or more isomerizations	Escherichia coli

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Release 2023.1 (January 2023)