Crystallization (Comment) | Organism |
---|---|
- |
Flavobacterium sp. |
Protein Variants | Comment | Organism |
---|---|---|
T152C | the autoproteolysis-active precursor is kinetically slower than the wild type enzyme | Flavobacterium sp. |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
glycine | reversible inhibitor | Flavobacterium sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Flavobacterium sp. | glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Flavobacterium sp. | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Flavobacterium sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | glycosylasparaginase protein is synthesized as a single-chain precursor (inhibitor-free precursor) and requires a cis proteolysis of its own main-chain amide bond, splitting it into two subunits. Once autocleaved, the mature glycosylasparaginase with a free amino end exposed at Thr152 becomes active in glycoprotein degradation by binding to and processing its glycoasparagine substrate | Flavobacterium sp. | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
glycosylasparaginase | - |
Flavobacterium sp. |