EC Number   |
General Information |
Reference |
|---|
   3.5.2.B2 | evolution |
the isochorismatase-like hydrolase (IHL, Mh33H4-5540, EC 3.3.2.1) with (+)-gamma-lactamase activity constitutes a distinct family of gamma-lactamase |
755471 |
| 3.5.2.B2 | more |
the enzyme crystal structures show that the binding sites of both (+) and (-)-gamma-lactam resemble those of isochorismatase-like hydrolases, but the cover loop conserved in isochorismatase-like hydrolases is lacking in the enzyme, probably resulting in its incomplete enantioselectivity. Structural, biochemical, and molecular dynamics simulation studies demonstrate that the steric clash caused by the binding-site residues, especially the side-chain of Cys111 reduces the binding affinity of (-)-gamma-lactam and possibly the catalytic efficiency, which might explain the different catalytic specificities of the enantiomers of gamma-lactam |
755471 |
| 3.5.2.B2 | physiological function |
(+)-gamma-lactamase catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir |
755471 |
| 3.5.2.B2 | physiological function |
gene deletion mutant shows hyphal growth on solid media comparable to the wild-type and significantly reduced growth on media supplied with 1,3-benzoxazol-2(3H)-one and 6-methoxy-1,3-benzoxazol-2(3H)-one |
-, 736167 |
