CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.20 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
|
3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Functional Family | Asparagine synthetase B |
Enzyme Information
| 6.3.5.4 |
Asparagine synthase (glutamine-hydrolyzing).
based on mapping to UniProt P22106
ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate.
-!- The enzyme from Escherichia coli has two active sites that are connected by an intramolecular ammonia tunnel. -!- The enzyme catalyzes three distinct chemical reactions: glutamine hydrolysis to yield ammonia takes place in the N-terminal domain. -!- The C-terminal active site mediates both the synthesis of a beta- aspartyl-AMP intermediate and its subsequent reaction with ammonia. -!- The ammonia released is channeled to the other active site to yield asparagine.
|
UniProtKB Entries (1)
| P22106 |
ASNB_ECOLI
Escherichia coli K-12
Asparagine synthetase B [glutamine-hydrolyzing]
|
PDB Structure
| PDB | 1CT9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
Biochemistry
|
