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Article

Mutational and structural analyses of Caldanaerobius polysaccharolyticus Man5B reveal novel active site residues for family 5 glycoside hydrolases.

PloS one - 1 Jan 2013

Oyama Takuji, Schmitz George E, Dodd Dylan, Han Yejun, Burnett Alanna, Nagasawa Naoko, Mackie Roderick I, Nakamura Haruki, Morikawa Kosuke, Cann Isaac

Abstract excerpt

CpMan5B is a glycoside hydrolase (GH) family 5 enzyme exhibiting both β-1,4-mannosidic and β-1,4-glucosidic cleavage activities. To provide insight into the amino acid residues that contribute to catalysis and substrate specificity, we solved the structure of CpMan5B at 1.6 Å resolution. The structure revealed several active site residues (Y12, N92 and R196) in CpMan5B that are not present in the active sites of...

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Identifiers

PMID: 24278284
DOI: 10.1371/journal.pone.0080448
PMCID: PMC3835425

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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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