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Article

Roles of asp126 and asp156 in the enzyme function of sphingomyelinase from Bacillus cereus.

Journal of biochemistry - 1 Jul 1999

Fujii S, Ogata K, Inoue B, Inoue S, Murakami M, Iwama S, Katsumura S, Tomita M, Tamura H, Tsukamoto K, Ikezawa H, Ikeda K

Abstract excerpt

To elucidate the roles of conserved Asp residues of Bacillus cereus sphingomyelinase (SMase) in the kinetic and binding properties of the enzyme toward various substrates and Mg2+, the kinetic data on mutant SMases (D126G and D156G) were compared with those of wild type (WT) enzyme. The stereoselectivity of the enzyme in the hydrolysis of monodispersed short-chain sphingomyelin (SM) analogs and the binding of...

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PMID: 10393325
DOI: 10.1093/oxfordjournals.jbchem.a022441

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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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