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Literature summary for 3.4.21.12 extracted from
- The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding (2002), Biochemistry, 41, 8860-8867.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | Pro region N-domain mutants: disruption of the hydrogen bonding potentials of Y26 and E30 primarily alters Pro binding to the folding transition state as compared to binding in the initial and native state complexes | Lysobacter enzymogenes |
General Stability
| General Stability | Organism |
|---|---|
| Pro N-domain both provides direct interactions with alpha-lytic protease that stabilize the folding transition state and confers stability to the Pro C-domain | Lysobacter enzymogenes |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Lysobacter enzymogenes | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lysobacter enzymogenes | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme is synthesized with a large, two-domain pro region (Pro) that catalyzes the folding of the protease to its native conformation. In the absence of its (Pro) folding catalyst, alpha-lytic protease encounters a very large folding barrier that effectively prevents the protease from folding. The extremely high alpha-lytic protease folding barrier necessitates the presence of both the (Pro) domains | Lysobacter enzymogenes |
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