Abstract:
:The ADPglucose pyrophosphorylases from Rhodopseudomonas sphaeroides and Rhodopseudomonas gelatinosa are activated by fructose-6-phosphate, pyruvate and fructose-1,6 biophosphate-P2. The effects of the activators are to increase significantly the Vmax of ADPglucose synthesis and to lower the S0.5 values (concentration of substrates giving 50% maximal velocity) for ATP and MgCl2. The R. sphaeroides enzyme is inhibited by Pi while the R. gelatinosa enzyme is inhibited by AMP as well as by Pi. The interaction between inhibitor and activator is complex. At very low concentrations of activator the enzyme is more sensitized to inhibition. However, at higher concentrations of activator there is a decrease in the sensitivity of the enzyme towards inhibition. The findings are discussed with respect to glycogen synthesis in these microorganisms and may be related to findings that indicate that Rhodopseudomonads have the ability to degrade sugars via the Entner-Duodoroff or Embden-Meyerhoff pathways.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Preiss J,Greenberg E,Parsons TF,Downey Jdoi
10.1007/BF00421887subject
Has Abstractpub_date
1980-05-01 00:00:00pages
21-31issue
1eissn
0302-8933issn
1432-072Xjournal_volume
126pub_type
杂志文章abstract::L-Alanine dehydrogenase was found in extracts of the antibiotic producer Streptomyces clavuligerus. The enzyme was induced by ammonia, and the level of induction was dependent on the extracellular concentraction. L-Alanine was the only amino acid able to induce alanine dehydrogenase. The enzyme was characterized from ...
journal_title:Archives of microbiology
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journal_title:Archives of microbiology
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pub_type: 杂志文章
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journal_title:Archives of microbiology
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doi:10.1007/s002030050392
更新日期:1996-11-01 00:00:00
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journal_title:Archives of microbiology
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journal_title:Archives of microbiology
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