N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships.
N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships.
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哈维氏弧菌的 N,N-二乙酰壳二糖酶。
DOI：
10.1016/s0021-9258(18)63767-6
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
J. Zyskind
中科院分区：
文献类型：
--
作者：
R. Soto;J. Zyskind
The nucleotide sequence of the gene,chb, encoding the outer membrane protein,N, N′-diacetylchitobiase (chitobiase), of the marine bacterium,Vibrio harveyi, has been determined. The amino acid sequence of prechitobiase was derived from the nucleotide sequence. Prechitobiase has a molecular mass of 97,771 Da and consists of 883 amino acid residues. A characteristic signal peptide is present at the amino terminus whose removal is inhibited by the antibiotic, globomycin, suggesting that mature chitobiase is a lipoprotein with a maturation pathway similar to that of theEscherichia colimajor outer membrane lipoprotein. A perfect homology to six amino acids at the processing and modification region of the outer membrane lipoprotein ofE. coliwas found with amino acids 15–19 of the deduced prechitobiase protein sequence. Chitobiase shares similarities and possibly common ancestry with the α-chain of the human β-hexosaminidase. A comparison of the amino acid sequences of chitobiase and the α-chain of β-hexosaminidase gave a highly significant alignment score of 19.1 standard deviation units above a mean randomized alignment score. Primer extension analysis of the promoter region revealed three transcription initiation sites used byE. colicells harboring thechbgene, two of which were also evident inV. harveyicells.
