EC Number   |
Posttranslational Modification |
Reference |
|---|
    4.1.1.19 | proteolytic modification |
a unique band of about 20 kDa representing uncleaved proenzyme is detected at 20 hours post-infection in L2 cells, with very little cleaved protein appearing. Over the next 24 hours, this ratio slowly shifted, and by 44 hours post-infection, the majority of protein is in the cleaved, active state |
727553 |
| 4.1.1.19 | proteolytic modification |
existence of an autocatalytic proteolytic property of ADC protein, which possibly regulates posttranslationally the levels and/or the activity of ADC enzyme |
657014 |
| 4.1.1.19 | proteolytic modification |
maximal activity of ADC1 in yeast requires the presence of general protease genes, and it is likely that dimer formation precedes proteolytic processing of the ADC pre-protein monomer |
656995 |
| 4.1.1.19 | proteolytic modification |
post-translational proteolysis of ADC depends on the presence of a protease-sensitive loop in the structure of the protein |
692241 |
| 4.1.1.19 | proteolytic modification |
synthesized as an inactive proenzyme |
-, 719521, 719848 |
| 4.1.1.19 | proteolytic modification |
the enzyme is formed by self-cleavage of a proenzyme into a 5000 Da subunit and a 12000 Da subunit that contains a reactive pyruvoyl group |
656053 |
| 4.1.1.19 | proteolytic modification |
the protein is synthesized as a 66000 Da precursor that is proteolytically processed into two polypeptides of 42000 and 24000 da |
656915 |
| 4.1.1.19 | proteolytic modification |
the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains. Asn47, Ser52, Ser53, Ile54, and Glu109 are proposed to play roles in the self-processing reaction |
657363 |
| 4.1.1.19 | proteolytic modification |
the recombinant enzyme self-cleaved to form a reactive pyruvoyl group, and the subunits assembled into a thermostable (alpha/beta)3 complex |
-, 680506 |
| 4.1.1.19 | pyruvoyl group formation |
the enzyme is synthesized as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue (Ser44) via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme |
719521 |
