Literature summary for 2.5.1.47 extracted from

Wirtz, M.; Heeg, C.; Samami, A.A.; Ruppert, T.; Hell, R.
Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include Nalpha-terminal acetylation (2010), Amino Acids, 39, 1077-1086.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue	Arabidopsis thaliana

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	isoforms OAS-TL A and B are the most abundant isoforms in all tissues analyzed. The major isoforms present in cytosol, plastids and mitochondria show significant modifications into up to seven subspecies. Specific isoforms are found to be differentially modified in the leaves, roots, stem and cell culture. Sulfur deficiency does not alter modification of enzyme proteins purified from cell culture that shows the highest complexity of modifications. However, the pattern of enzyme modification is found to be stable within an analyzed tissue	Arabidopsis thaliana	-

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Release 2023.1 (January 2023)