Literature summary for 2.3.1.30 extracted from

Zhao, C.; Moriga, Y.; Feng, B.; Kumada, Y.; Imanaka, H.; Imamura, K.; Nakanishi, K.
On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli (2006), Biochem. Biophys. Res. Commun., 341, 911-916.

Search for more literature for 2.3.1.30

Protein Variants

Protein Variants	Comment	Organism
del266T-273I	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
del268E-273I	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
del270G-273I	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
delI273	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
delI273I/delG272	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
I273A	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli
I273E	no complex formation with O-acetylserine sulfhydrylase A	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Subunits

Subunits	Comment	Organism
More	cysteine synthase from Escherichia coli is a bienzyme complex comprised of serine acetyltransferase and O-acetylserine sulfhydrylase A. The C-terminus of SAT, Ile273, along with Glu268 and Asp271, is essential for complex formation	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)