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Article

Modulation of substrate preference of thermus maltogenic amylase by mutation of the residues at the interface of a dimer.

Bioscience, biotechnology, and biochemistry - 1 Jun 2007

Park Sung-Hoon, Kang Hee-Kwon, Shim Jae-Hoon, Woo Eui-Jeon, Hong Jung-Sun, Kim Jung-Wan, Oh Byung-Ha, Lee Byong Hoon, Cha Hyunju, Park Kwan-Hwa

Abstract excerpt

To elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The k(cat)/K(m) value of the mutant for amylose increased signi...

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Source

Identifiers

PMID: 17587692
DOI: 10.1271/bbb.70017

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17587692-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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