TY  - BOOK
AU  - Bokma E
AU  - Barends T
AU  - Beintema J J
AU  - Dijkstra B W
AU  - Scheltinga A C T VAN
TI  - Enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis
PY  - 2000///
PB  - FEBS Letters
KW  - Enzyme kinetics
KW  - Hevamine
KW  - Hevea brasiliensis
N1  - Source Year: 2001
N2  - The enzyme kinetics of hevamine, a chitinase from the rubber tree Hevea brasiliensis, were studied in detail with a new enzyme assay. In this assay, the enzyme reaction products were derivatized by reductive coupling to a chromophore. Products were separated by HPLC and the amount of product was calculated by peak integration. Penta-N-acetylglucosamine (penta-nag) and hexa-N-acetylglucosamine (hexa-nag) were used as substrates. Hexa-nag was more efficiently converted than penta-nag, which is an indication that hevamine has at least six sugar binding sites in the activesite. Tetra-N-acetylglucosamine (tetra-nag) and allosamidin were tested as inhibitors. Allosamidin was found to be a competitive inhibitor with aKi of 3.1mM. Under the conditions tested, tetra-nag did not inhibit hevamine
UR  - CPA
ER  -