A single amino acid substitution can shift the optimum pH of DNase I for enzyme activity: biochemical and molecular analysis of the piscine DNase I family.
作者： T Yasuda , H Takeshita , R Iida , M Ueki , T Nakajima
DOI: 10.1016/J.BBAGEN.2004.03.012
关键词:
摘要: We purified four piscine deoxyribonucleases I (DNases I) from Anguilla japonica, Pagrus major, Cryprus carpio and Oreochromis mossambica. The enzymes had an optimum pH for activity of approximately 8.0, significantly higher than those mammalian enzymes. cDNAs encoding the first three these DNases were cloned, sequence Takifugu rubripes enzyme was obtained a database search. Nucleotide analyses revealed relatively greater structural variations among DNase family other vertebrate families. From comparison their catalytic properties, could be classified into two groups: low-pH group, such as enzymes, with 6.5-7.0, high-pH reptile, amphibian 8.0. His residue at position 44 former group is replaced by Asp in latter. Replacement Asp44 decreased to value similar that group. Therefore, Asp44His might involved evolutionarily critical change I.
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