CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1170 | L-asparaginase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | L-asparaginase, N-terminal domain |
| Functional Family | L-asparaginase 2 |
Enzyme Information
| 3.5.1.38 |
Glutamin-(asparagin-)ase.
based on mapping to UniProt P10182
(1) L-glutamine + H(2)O = L-glutamate + NH(3). (2) L-asparagine + H(2)O = L-aspartate + NH(3).
-!- L-asparagine is hydrolyzed at 0.8 of the rate of L-glutamine. -!- The D-isomers are also hydrolyzed, more slowly. -!- Cf. EC 3.5.1.1 and EC 3.5.1.2.
|
UniProtKB Entries (1)
| P10182 |
ASPQ_PSES7
Pseudomonas sp. ATCC29598
Glutaminase-asparaginase
|
PDB Structure
| PDB | 1DJO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu.
Biochemistry
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