Literature summary for 2.5.1.47 extracted from

Wawrzynska, A.; Kurzyk, A.; Mierzwinska, M.; Plochocka, D.; Wieczorek, G.; Sirko, A.
Direct targeting of Arabidopsis cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis (2013), Plant Sci., 207, 148-157.

Search for more literature for 2.5.1.47

Cloned(Commentary)

Cloned (Comment)	Organism
gene OASC, ssemi-quantitative RT-PCR isozyme expression analysis	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
additional information	direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis and enhance cysteine rduction. Several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for serine acetyltransferase binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation. Transgenic Arabidopsis lines with PEP4 expression show moderate changes in SAT and OAS-TL activities	Arabidopsis thaliana

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	isozyme OAS-TL C	Arabidopsis thaliana	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Arabidopsis thaliana	the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity	?	-	?
O-acetyl-L-serine + hydrogen sulfide	Arabidopsis thaliana	-	L-cysteine + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q43725	isozyme OAS-TL C; gene OASC	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the mitochondrial isozyme OAS-TL C accounts for less than 5% of total OAS-TL activity	Arabidopsis thaliana	?	-	?
O-acetyl-L-serine + hydrogen sulfide	-	Arabidopsis thaliana	L-cysteine + acetate	-	?

Synonyms

Synonyms	Comment	Organism
O-acetylserine (thiol) lyase	-	Arabidopsis thaliana
O3-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase	-	Arabidopsis thaliana
OAS-TL C	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
malfunction	direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis. OAS-TL C loss-of-function mutant shows a retarded growth phenotype, conversely to the loss-of-function mutants for OAS-TL A and OAS-TL B	Arabidopsis thaliana
metabolism	biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific protein-protein interactions influencing the rate of cysteine production. The enzyme activity and level of thiols are not influenced by PEP4 expression. Increased serine acetyltransferase activity, but not O-acetylserine (thiol) lyase activity is an efficient trigger for enhanced cysteine synthesis in planta	Arabidopsis thaliana
additional information	computational modeling is used to build a model of the Arabidopsis thaliana mitochondrial cysteine synthase complex, overview. Direct targeting of Arabidopsis thaliana cysteine synthase complexes with synthetic polypeptides to selectively deregulate cysteine synthesis, several polypeptides based on OAS-TL C amino-acid sequence found at SAT-OASTL interaction sites are designed as probable competitors for SAT binding. After verification of the binding in a yeast two-hybrid assay, the most strongly interacting polypeptide is introduced to different cellular compartments of Arabidopsis thaliana cell via genetic transformation	Arabidopsis thaliana
physiological function	biosynthesis of cysteine is one of the fundamental processes in plants providing the reduced sulfur for cell metabolism. It is accomplished by the sequential action of two enzymes, serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL). Together they constitute the hetero-oligomeric cysteine synthase (CS) complex through specific proteinprotein interactions influencing the rate of cysteine production. The function of the complex formation is not metabolic channeling, but sensing the sulfur status of the cell to properly adjust the sulfur homeostasis. Whereas OAS-TL is only active outside the CS complex, SAT is strongly activated by association with OAS-TL. Mitochondrial isozyme OAS-TL C has an additional function besides cysteine synthesis, regulatory function when complexed with serine acetyltransferase. The formation of the CS complex is also important because of the inhibition of the free serine acetyltransferase by cysteine	Arabidopsis thaliana

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Release 2023.1 (January 2023)