EC Number   |
Reference |
|---|
    3.4.13.22 | - |
683586 |
| 3.4.13.22 | crystal structures of VanXY mutant D59S and VanXY wild-type in apo and transition state analog-bound forms and of the mutant in complex with the D-Ala-D-Ala substrate and D-Ala product. Structural and biochemical analysis identifies the molecular determinants of VanXY dual specificity acting on dipeptide D-Ala-D-Ala or pentapeptide UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala, respectively. VanXY residues 110-115 form a mobile cap over the catalytic site, whose flexibility is involved in the switch between di- and pentapeptide hydrolysis. VanY pentapeptidases lack this element, which promotes binding of the penta- rather than that of the dipeptide |
732831 |
| 3.4.13.22 | enzyme crystallizes as a linear homohexamer which is held together by electrostatic interactions and H-bonding, and each subunit binds one Zn2+. The active site if VanX is in a cavity of 150 A that can only accomodate small molecules which explains the narrow substrate specificity of the enzyme. The Zn2+ is coordinated in a destorted tetrahedral arrangement with the side chains of His116, His184, Asp123 and a solvent water |
683534 |
| 3.4.13.22 | enzyme-D-Ala complex, enzyme-D-Ala-D-Ala complex, and enzyme in complex with phosphonate and phosphinate transition-state analogue inhibitors, complexsitting drops, 10 mg/ml protein, plus equal volume of precipitant solution: 0.25 M ammonium sulfate, 25% w/v polyethylene glycol monomethyl ester 5000, 0.1 M MES, 1 mM ZnCl2, X-ray diffraction at 2.1 A resolution structure determination and analysis |
653196 |
