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Results 1 - 3 of 3
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.16acetylation Streptomyces lividans GCN5-typeN-acetyltransferase SlPatA acetylates the enzyme at the active-site residue Lys617, the acetylation inactivates the enzyme, overview. Acetylated SlAacS is deacetylated by a sirtuin-type protein deacetylase. SlAacS acetylation/deacetylation may represent a conserved mechanism for regulation of acetoacetyl-CoA synthetase activity in all domains of life -, 728335
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.16proteolytic modification enzyme AACS is posttranslationally regulated, being cleaved at a specific site in the kidney. In vivo cleavage of enzyme AACS by legumain in HEK 293 cells generates the 55 kDa product from AACS. Incubation of recombinant AACS with recombinant legumain results in the degradation of AACS, optimally at pH 4.5. Knockdown of legumain with short-hairpin RNA against legumain using the hydrodynamics method leads to a decrease in the 55 kDa band of AACS in mouse kidney. Legumain is involved in the processing of AACS through the lysosomal degradation pathway in the kidney. Suppression of legumain results in a decrease in the cleaved form of AACS protein, and an increase in the full-length form of AACS protein. Legumain is involved in the cleavage of AACS in the kidney, suggesting that AACS is degraded by the lysosomal pathway -, 744226
Display the word mapDisplay the reaction diagram Show all sequences 6.2.1.16proteolytic modification site-specific cleavage at residue AACS Asn503 and Asn547 of acetoacetyl-CoA synthetase by recombinant autoactivated legumain, a lysosomal asparaginyl endopeptidase, at pH 5.0 and 30°C. The cleaved form of AACS (1-547) loses the ability to convert acetoacetate to acetoacetyl-CoA. AACS is cleaved by legumain in the liver and the kidney to give two primary bands of approximately 56 kDa and 48 kDa, AACS (1-547) and AACS (1-503) are approximately 56 kDa and 55 kDa, respectively. The cleavage site for the formation of the 56-kDa product is located in the C-terminal side region from amino acid 487, whereas that of the 48-kDa product is located in the N-terminal side region from amino acid 468 744906
Results 1 - 3 of 3