CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.40
Functional Family Glutaminase-asparaginase

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 4PGA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution.
Jakob, C.G., Lewinski, K., LaCount, M.W., Roberts, J., Lebioda, L.
Biochemistry