Active site glutamate

Leimkiihler S, AL Stockert, K Igarashi, T Nishino, R Hille (2004) The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. J Biol Chem 279 40437-40444. 

The structure of dihydroneopterin aldolase has been analyzed further with respect to the functional roles of conserved active site glutamate and lysine residues <2006B15232>. NMR studies have also suggested that the isomerization of dihydroneopterin to dihydromonapterin catalyzed by the same enzyme involves the action of the same functional groups <2007MI2240>. 

G. Muller-Newen, U. Janssen, and W. Stoffel, Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue, Eur.J. Biochem. 1995, 228, 68-73. 

The acid-base catalytic machinery shows slight variations within families. Thus, the active site glutamate in the GH 3 p-glucosidase labelled by A-bromoacetylglucosylamine is not strictly conserved in GH 3, and there individual members of GH 1 and GH 2 which have difierent acid or base catalysts than the majority. 

Davoodi, J., Wakarchuk, W.W., Campbell, R.L., Garey, P.R., Surewicz, W.K. Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions. Eur. J. Biochem. 1995,232, 839 3. 

This catalysis is probably a combination of transition state stabilisation by the intact active site, as well as general base catalysis by the other active site glutamate, enhancing the nucleophUicity of the acceptor. It is posmlated [35] that the mutant serine residue stabilises the glycosylation transition state by neutralising... 

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