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Article

Substrate recognition mechanism of thermophilic dual-substrate enzyme.

Journal of biochemistry - 1 Jul 2001

Ura H, Nakai T, Kawaguchi S I, Miyahara I, Hirotsu K, Kuramitsu S

Abstract excerpt

Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic...

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Source

Identifiers

PMID: 11432784
DOI: 10.1093/oxfordjournals.jbchem.a002966

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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