Article
Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis.
The Journal of biological chemistry - 7 Aug 1998
Guo H C, Xu Q, Buckley D, Guan C
Abstract excerpt
Glycosylasparaginase (GA) is a member of a novel family of N-terminal nucleophile hydrolases that catalytically use an N-terminal residue as both a polarizing base and a nucleophile. These enzymes are activated from a single chain precursor by intramolecular autoproteolysis to yield the N-termina...
Topics
- Amino Acid Sequence
- Aspartylglucosylaminase
- Bacterial Proteins
- Binding Sites
- Crystallography, X-Ray
- Dimerization
- Flavobacterium
- Humans
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Recombinant Proteins
- Sequence Alignment
