Shirokizawa O, Akiba T, Horikoshi K
Superbugs Project, Research Development Corporation of Japan, Tokyo.
FEMS Microbiol Lett. 1990 Jul;58(2):131-5. doi: 10.1111/j.1574-6968.1990.tb13965.x.
The nucleotide sequence of the G6-amylase gene from alkalophilic Bacillus sp. H-167 was determined. The open reading frame of the gene consisted of 2865 base pairs, encoding 955 amino acids. The NH2-terminal amino acid sequence analysis of the G6-amylase indicated that the enzyme had a single peptide of 33 amino acid residues and the mature enzyme was composed of 922 amino acids, giving a molecular mass of 102,598. Identity of the NH2-terminal amino acid sequences among each component of the multiform G6-amylase suggested the proteolytic processing of the COOH-terminal side of the enzyme. The DNA sequence and the deduced amino acid sequence of the G6-amylase gene showed no homology with those of other bacterial alpha-amylases although the consensus amino acid sequences of the active center were well conserved.
测定了嗜碱芽孢杆菌H-167的G6-淀粉酶基因的核苷酸序列。该基因的开放阅读框由2865个碱基对组成，编码955个氨基酸。G6-淀粉酶的NH2-末端氨基酸序列分析表明，该酶有一个由33个氨基酸残基组成的单一肽段，成熟酶由922个氨基酸组成，分子量为102598。多形G6-淀粉酶各组分之间NH2-末端氨基酸序列的一致性表明该酶COOH-末端存在蛋白水解加工。G6-淀粉酶基因的DNA序列和推导的氨基酸序列与其他细菌α-淀粉酶的序列没有同源性，尽管活性中心的共有氨基酸序列保守性良好。
