Actinomycete metabolism: α-phenylmannosidase of <i>Streptomyces griseus</i>

Hockenhull, D. J. D.; Ashton, G. C.; Fantes, K. H.; Whitehead, Belinda

doi:10.1042/bj0570093

Cited by 22 publications

(16 citation statements)

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“…Towards the termination of the production stage less than 10% may be found (HOCKENHULL,1963). This conversion of the mannosidostreptomycin to streptomycin has been found to correlate well with the appearance and increasing concentration of an ex-mannosidostreptomycinase in the broth (PERLMAN and LANGLYKKE, 1948;HOCKENHULL et at., 1954a;MARUTA and TANAKA, 1957). The properties of the enzyme have been studied by several investigators.…”

Section: Formation Of the Glycosidic Bondsmentioning

confidence: 87%

“…(PERLMAN and LANGLYKKE, 1948;HOCKENHULL et at., 1954a;SHAW et at., 1960). The enzyme was also inhibited by anaerobic conditions and certain organic compounds (HOCKENHULL et at., 1954a;KOLLAR, 1957). Inhibition by sugars and their derivatives has been observed.…”

Section: Mannosidostreptomycin Synthesis and Hydrolysismentioning

confidence: 93%

“…The metal ions, Cu 2 +, Hg2+ Fe 2 +, NiH, Zn 2 + and Cr6+ were found to inhibit the enzyme. (PERLMAN and LANGLYKKE, 1948;HOCKENHULL et at., 1954a;SHAW et at., 1960). The enzyme was also inhibited by anaerobic conditions and certain organic compounds (HOCKENHULL et at., 1954a;KOLLAR, 1957).…”

Section: Mannosidostreptomycin Synthesis and Hydrolysismentioning

confidence: 94%

“…The optimum pH of the enzyme has been reported to be approximately 8 (PERLMAN and LANGLYKKE, 1948;HOCKENHULL et at., 1954a), 7.6-7.7 (KOLLAR, 1958a) and 6.8-7.4 (MAR UTA and TANAKA, 1957). The optimum temperature has been reported at 40C (HOCKENHULL et at., 1954a;KOLLAR, 1958a). …”

Section: Formation Of the Glycosidic Bondsmentioning

confidence: 96%

“…Evidence has been obtained that the enzyme will also catalyze the hydrolysis of phenyl-ex-D-mannoside to phenol and D-mannose (HOCKENHULL et at., 1954a). The optimum pH of the enzyme has been reported to be approximately 8 (PERLMAN and LANGLYKKE, 1948;HOCKENHULL et at., 1954a), 7.6-7.7 (KOLLAR, 1958a) and 6.8-7.4 (MAR UTA and TANAKA, 1957). The optimum temperature has been reported at 40C (HOCKENHULL et at., 1954a;KOLLAR, 1958a).…”

Section: Formation Of the Glycosidic Bondsmentioning

confidence: 96%

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Biosynthesis

1967

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All rights, especially that of translation into f oreign 1anguages, reserved. It is also forbidden to reproduce this book, either who1e or in part, by photomechanical means (photostat, microfilm and/or microcard) or by other procedure without written pennission from Springcr-Vcrlag Berlin Heide1bCig GmbH. DedicationFor most areas of scientific pursuit, there is usually that rare investigator who has the imagination to conceive ideas, who has faith in his visions, and who has the ability to critically test his concepts in the laboratory. Almost invariably, this scientist also inspires younger men to enthusiastically enter into his research program. To him should go the accolades and the recognitions of the esteem in which he is held. As only a small part of this esteem, we wish to dedicate these books to Professor SELMAN A. W AKSMAN in appreciation of his leadership and contributions in all facets of antibiotic research. PrefaceThe idea for publishing these books on the mechanism of action and on the biosynthesis of antibiotics was born of frustration in our attempts to keep abreast of the literature. Gone were the years when we were able to keep a bibliography on antibiotics and feel confident that we could find everything that was being published on this sUbject. These fields of investigation were moving forward so rapidly and were encompassing so wide a range of specialized areas in microbiology and chemistry that it was almost impossible to keep abreast of developments. In our naivete and enthusiasm, however, we were unaware that we were toying with an idea that might enmesh us, that we were creating an entity with a life of its own, that we were letting loose a Golom who instead of being our servant would be our master.That we set up ideals for these books is obvious; they would be current guides to developments and information in the areas of mechanism of action and biosynthesis of antibiotics. For almost every subject, we wished to enlist the aid of an investigator who himself had played a part in determining the nature of the phenomena that were being discussed. One concept for the books was that they include only antibiotics for which a definitive, well-documented mechanism of action or biosynthetic pathway was known. Yet, such an approach would not entirely serve the purpose we projected, for it would not encompass all of the information available in these fields of antibiotic investigations and blind searches for the original literature would still have to be made. We therefore chose to include any and all antibiotics about which some pertinent information had been published. It was obvious even at the start that such a compilation, integration, and analysis of information could never be complete unless scientific investigations ceased at the moment the last manuscript was submitted-an end that was neither desirable nor possible. An addendum was therefore included at the end of the volume and left open for the addition of new information until the last pages of the regular articles had been printed.The...

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Section: Formation Of the Glycosidic Bondsmentioning

confidence: 87%

Section: Mannosidostreptomycin Synthesis and Hydrolysismentioning

confidence: 93%

Section: Mannosidostreptomycin Synthesis and Hydrolysismentioning

confidence: 94%

Section: Formation Of the Glycosidic Bondsmentioning

confidence: 96%

Section: Formation Of the Glycosidic Bondsmentioning

confidence: 96%

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Biosynthesis

1967

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Location and action of Streptomyces griseus α‐D‐mannosidase, an antibiotic‐transforming enzyme

Inamine

Demain

1970

Biotech & Bioengineering

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SummaryStreptornyces 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. Methyla-D-mannoside was found to be a strong inhibitor of the hydrolysis of both p-nitrophenyla-D-mannoside and mannosidostreptomycin. The enzyme is bound a t or near the surface of the cell and is inactivated by sonic oscillation. Small particulate matter containing most of the activity can be released from the cells into water, such release being inhibited by phosphate, Tris, or sodium chloride.

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Streptomycin

Horner¹

1967

Biosynthesis

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Actinomycete metabolism: α-phenylmannosidase of Streptomyces griseus

Cited by 22 publications

References 4 publications

Biosynthesis

Biosynthesis

Location and action of Streptomyces griseus α‐D‐mannosidase, an antibiotic‐transforming enzyme

Streptomycin

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