Properties of the reversible nonoxidative vanillate/4-hydroxybenzoate decarboxylase from Bacillus subtilis.

摘要: Bacillus subtilis (ATCC 6051) reversibly decarboxylates vanillate and 4-hydroxybenzoate under both aerobic anoxic conditions. Thus, we have identified on the basis of gene sequence homology with Sedimentibacter hydroxybenzoicus Streptomyces sp. strain D7, a putative B. hydroxybenzoate decarboxylase. The native form this enzyme is encoded by 3 genes yclBCD (GI Sequence Identification Nos.: 2632649, 2632650, 2632651) that renamed during research as bsdBCD to align existing nomenclature. bsdD reported in database be 690 bp; however, our analysis revealed size fact 228 bp, an observation results shortening YclD (i.e., BsdD) from 229 75 aa. corresponding were cloned into Escherichia coli, heterologously expressed was assayed for activity. decarboxylase exhibited narrow substrate range, only 2 tested substrates, (Kmapp = 4 mmol.L-1) ~1 mmol.L-1), being decarboxylated. recombinant had properties similar respect specific activity, kinetic properties, bidirectional decarboxylase-carboxylase oxygen insensitivity, specificity.