谷氨酸脱氢酶
NAD+激酶
生物化学
肽序列
辅因子
生物
酶
脱氢酶
氨基酸
核酸序列
序列(生物学)
谷氨酸受体
基因
受体
作者
Kathryn S. Lilley,Patrick J. Baker,K.L. Britton,Timothy J. Stillman,Paul E. Brown,Arthur J. G. Moir,Paul C. Engel,David W. Rice,John Bell,Evelyn T. Bell
标识
DOI:10.1016/0167-4838(91)90001-g
摘要
The amino acid sequence is reported for CNBr and tryptic peptide fragments of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum. Together with the N-terminal sequence, these make up about 75% of the total sequence. The sequence shows extensive similarity with that of the NADP(+)-dependent glutamate dehydrogenase of Escherichia coli (52% identical residues out of the 332 compared) allowing confident placing of the peptide fragments within the overall sequence. This demonstrated sequence similarity with the E. coli enzyme, despite different coenzyme specificity, is much greater than the similarity (31% identities) between the GDH's of C. symbiosum and Peptostreptococcus asaccharolyticus, both NAD(+)-linked. The evolutionary implications are discussed. In the 'fingerprint' region of the nucleotide binding fold the sequence Gly X Gly X X Ala is found, rather than Gly X Gly X X Gly. The sequence found here has previously been associated with NADP+ specificity and its finding in a strictly NAD(+)-dependent enzyme requires closer examination of the function of this structural motif.
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