CATH Classification

Domain Context

CATH Clusters

Superfamily HUPs
Functional Family Asparagine synthase 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.
Larsen, T.M., Boehlein, S.K., Schuster, S.M., Richards, N.G., Thoden, J.B., Holden, H.M., Rayment, I.
Biochemistry