Glycine-assisted enhancement of 1,4-beta-d-xylan xylanohydrolase activity at alkaline pH with a pH optimum shift.
This is the first report describing the enhancement of xylanase activity by the neutral amino acid glycine. Xylanase activity is increased seven-fold at alkaline pH in the presence of glycine and its pH optimum is shifted from pH 7 to 8 without using any protein engineering techniques. Analysis of the steady-state kinetics revealed that glycine in the reaction mixture increases the K(m) and k(cat) values of the enzyme. Chemoaffinity labeling and studies using glycine esters indicate an involvement of the carboxylate ion of glycine in enhancing xylanase catalytic activity. A novel possible mechanism for the glycine-assisted catalytic action of xylanase is proposed.
Vathipadiekal
Vinod
V
Division of Biochemical Sciences, National Chemical Laboratory, Pune 41108, India.
Verma
Anamika
A
Rao
Mala
M
D002384:Catalysis; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry / Q000378:metabolism*; D004789:Enzyme Activation; D005998:Glycine / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D015394:Molecular Structure; D013050:Spectrometry, Fluorescence; D014990:Xylans / Q000737:chemistry / Q000378:metabolism*
D014990:Xylans; D043364:Endo-1,4-beta Xylanases; D005998:Glycine