Asset Details
Do you wish to reserve the book?
Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase
Do you wish to request the book?
Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Cysteine biosynthesis in Lactobacillus casei: identification and characterization of a serine acetyltransferase
2016
Overview
In bacteria, cysteine can be synthesized from serine by two steps involving an L-serine O-acetyltransferase (SAT) and a cysteine synthase (CysK). While CysK is found in the publicly available annotated genome from Lactobacillus casei ATCC 334, a gene encoding SAT (cysE) is missing. In this study, we found that various strains of L. casei grew in a chemically defined medium containing sulfide as the sole sulfur source, indicating the presence of a serine O-acetyltransferase. The gene lying upstream of cysK is predicted to encode a homoserine trans-succinylase (metA). To study the function of this gene, it was cloned from L. casei FAM18110. The purified, recombinant protein did not acylate L-homoserine in vitro. Instead, it catalyzed the formation of O-acetyl serine from L-serine and acetyl-CoA. Furthermore, the plasmid expressing the L. casei gene complemented an Escherichia coli cysE mutant strain but not an E. coli metA mutant. This clearly demonstrated that the gene annotated as metA in fact encodes the SAT function and should be annotated as cysE.
A gene that is annotated as homoserine succinyltransferase actually encodes a serine acetyltransferase in Lactobacillus casei.
Publisher
Oxford University Press
Subject
Acetyl Coenzyme A - metabolism
/ Cysteine
/ Cysteine Synthase - metabolism
/ E coli
/ Genomes
/ L-Serine
/ Lactobacillus casei - enzymology
/ Lactobacillus casei - genetics
/ Lactobacillus casei - metabolism
/ Molecular Sequence Annotation
/ Mutants
/ Mutation
/ Plasmids
/ Recombinant Proteins - metabolism
/ Serine - analogs & derivatives
/ Serine O-Acetyltransferase - genetics
/ Serine O-Acetyltransferase - isolation & purification
/ Serine O-Acetyltransferase - metabolism
/ Sulfides
/ Sulfur
