D175 DISCRIMINATES BETWEEN NADH AND NADPH IN THE COENZYME BINDING-SITE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS D-LACTATE DEHYDROGENASE

作者：BERNARD N; JOHNSEN K; HOLBROOK JJ; DELCOUR J

来源：Biochemical and Biophysical Research Communications, 1995, 208(3): 895-900.

DOI：10.1006/bbrc.1995.1419

The NAD-dependent D-(-)-lactate dehydrogenase (D-LDH) from Lactobacillus delbrueckii subsp. bulgaricus (in short, L. bulgaricus) has been modified at position 175 by site-directed mutagenesis, changing a conserved aspartate residue into an alanine. The D175A mutant enzyme displays a 40-fold shift in coenzyme preference from NADH to NADPH. This demonstrates that D175 truly belongs to the amino acid consensus GXGXXGX((17))D (where X represents any residue) which is the signature of the coenzyme binding site of most NAD-dependent dehydrogenases.

• 出版日期1995-3-28