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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.47 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

EC Number Inhibitors Comment Organism Structure
2.5.1.47 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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.5.1.47 leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.47 pyridoxal 5'-phosphate
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
2.5.1.47 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
2.5.1.47 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
2.5.1.47 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
2.5.1.47 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 protein–protein 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