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ABSTRACT:
SUBMITTER: Tomonaga Y
PROVIDER: S-EPMC5668673 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Tomonaga Yoshihisa Y Kaneko Ryosuke R Goto Masaru M Ohshima Toshihisa T Yoshimune Kazuaki K
Biochemistry and biophysics reports 20150715
Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon <i>Sulfolobus tokodaii</i> was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) i ...[more]