EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.3.1.35 | proteolytic modification |
autoproteolysis occurs between A194/T195, which results in generation of alpha and beta polypeptides |
754657 |
| 2.3.1.35 | proteolytic modification |
enzyme belongs to the N-terminal nucleophile hydrolase class of self-processing acetyltransferases |
660991 |
| 2.3.1.35 | proteolytic modification |
enzyme MtArgJ belongs to the N-terminal nucleophile (Ntn) fold class of enzymes, synthesized as a 404-amino acid long protein, which undergoes an autoproteolysis event between the Ala199 and Thr200. This autoproteolysis generates two fragments of approximately equal size (20-21 kDa), which then associate to form a protomeric unit (AB-heterodimer; A2B2 tetramer-dimer of the heterodimer) |
-, 756592 |
| 2.3.1.35 | proteolytic modification |
the arginine biosynthesis bifunctional protein ArgJ is cleaved via autoproteolysis into the arginine biosynthesis bifunctional protein ArgJ alpha chain and the arginine biosynthesis bifunctional protein ArgJ beta chain, which include the activities of glutamate N-acetyltransferase (EC 2.3.1.35, i.e. ornithine acetyltransferase, OATase, or ornithine transacetylase) and amino-acid acetyltransferase (EC 2.3.1.1, i.e. N-acetylglutamate synthase or AGSase) |
-, 756237, 757355 |
| 2.3.1.35 | proteolytic modification |
the two subunits withj molecular masses of 21300 Da and 23500 Da are derived from a single precursor polypeptide, suggesting that the CLGAT precursor is cleaved autocatalytically at the conserved ATML motif. The first 26-amino acid sequence at the N-terminus of the precursor functions as a chloroplast transit peptide |
673532 |
