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Location and action of Streptomyces griseus α‐ D ‐mannosidase, an antibiotic‐transforming enzyme
Author(s) -
Inamine Edward,
Demain Arnold L.
Publication year - 1970
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260120203
Subject(s) - enzyme , chemistry , streptomyces griseus , enzyme assay , hydrolysis , divalent , biochemistry , streptomyces albus , streptomyces , bacteria , biology , organic chemistry , genetics
Abstract Streptomyces mannosidase, like the enzyme from other sources, is shown to require a divalent cation for enzyme activity. N‐Ethylmaleimide pretreatment of enzyme‐containing cells eliminated the requirement of aeration for enzyme activity. Methyl‐α‐D‐mannoside was found to be a strong inhibitor of the hydrolysis of both p‐nitrophenyl‐α‐D‐mannoside and mannosidost reptomycin. The enzyme is bound at or near the surface of the cell and is inactivated by sonic oscillation. Small participate matter containing most of the activity can be released from the cells into water, such release being inhibited by phosphate, Tris, or sodium chloride.