Bacillus licheniformis MC14 alkaline phosphatase I gene with an extended COOH-terminus.
Bacillus licheniformis MC14 alkaline phosphatase I gene with an extended COOH-terminus.
复制标题
地衣芽孢杆菌 MC14 碱性磷酸酶 I 基因,具有延长的 COOH 末端。
DOI:
10.1111/j.1574-6968.1998.tb12840.x
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发表时间:
1998
影响因子:
2.1
通讯作者:
Hulett,FM
中科院分区:
文献类型:
--
作者:
Kim,JW;Peterson,T;Bee,G;Hulett,FM
Bacterial alkaline phosphatases (APases), except those isolated fromBacillus licheniformis, are approximately 45-kDa proteins while eucaryotic alkaline phosphatases are 60 kDa. To answer the question of whether the apparent 60-kDa alkaline phosphatase fromBacillus licheniformisaccurately reflected the size of the protein, the entire gene was analyzed. DNA sequence analysis of the alkaline phosphatase I (APaseI) gene ofB. licheniformisMC14 indicated that the gene could code for a 60-kDa protein of 553 amino acids. The deduced protein sequence of APaseI showed about 32% identity to those ofB. subtilisAPase III and IV and had apparent sequence homologies in the core structure and active sites that are conserved among APases of various sources. The extra carboxy-terminal sequence of APaseI, which made the enzyme bigger than other procaryotic APases, was not homologous to those of eucaryotic APases. The amino acid composition of APaseI was most similar to that of salt-dependent APase among the isozymes ofB. licheniformisMC14. Another open reading frame of 261 amino acids was present 142 nucleotide upstream of the APaseI gene and its predicted amino acid sequence showed 68% identity to that of glucose dehydrogenase ofB. megaterium.