Yoon, HS Kwon, S Han, MS Yu, Yeon-Gyu Yoon, MY 2024-01-21T12:05:07Z 2024-01-21T12:05:07Z 2021-09-04 2001-08 1017-7825 https://pubs.kist.re.kr/handle/201004/140294 To elucidate the putative role of the amido group in the metal binding of the fuculose-1-phosphate aldolase from Methanococcus jannaschii, we have examined a potential target using site-directed mutagenesis. The replacement of asparagine 25 with leucine or threonine was shown to have a negative effect, not only on catalytic efficiency, but also on substrate recognition as well. The Hill coefficient values yielded a value of approximate to1. All metals used with the wild-type aldolases exhibited higher activity than that of the mutants. The spectra of the mutants were quite different from the wildtype aldolase. A highly conserved amino acid of asparagine 25 in a related family of aldolase does not appear to provide sufficient evidence for evolution. English KOREAN SOC APPLIED MICROBIOLOGY AQUIFEX PYROPHILUS ESCHERICHIA-COLI CLASS-II OVERPRODUCTION PURIFICATION THERMOPHILE SPECIFICITY MECHANISM ENZYMES Mutagenic characterization of a conserved functional amino acid in fuculose-1-phosphate aldolase from Methanococcus jannaschii, a hyperthermophic archaea Article 1 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.11, no.4, pp.709 - 711 JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 11 4 709 711 scie scopus kci other 000170841600025 Biotechnology & Applied Microbiology Microbiology Biotechnology & Applied Microbiology Microbiology Article AQUIFEX PYROPHILUS ESCHERICHIA-COLI CLASS-II OVERPRODUCTION PURIFICATION THERMOPHILE SPECIFICITY MECHANISM ENZYMES aldolase site-directed mutagenesis Methanococcus jannaschii