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[Enzymatic study of citrate-isocitrate accumulation in yeast with glucose as the carbon source].
Z Allg Mikrobiol. 1983; 23(2):75-80.ZA

Abstract

The connection between the kinetics of citrate-isocitrate overproduction by Saccharomycopsis lipolytica in glucose media and the specific activities of the enzymes being related to overproduction has been investigated. The specific activities of citrate synthase, aconitate hydratase, NAD+-linked and NADP+-linked isocitrate dehydrogenase decline significantly after exhaustion of the nitrogen source, whereas the activity of the pyruvate carboxylase remains relatively constant and corresponds to changes of the production rate. The results are compared with those obtained by fermentations in n-alkane media and discussed in relation to mechanisms of overproduction.

Authors

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Pub Type(s)

English Abstract
Journal Article

Language

ger

PubMed ID

6868652

Citation

Franke-Rinker, D, et al. "[Enzymatic Study of Citrate-isocitrate Accumulation in Yeast With Glucose as the Carbon Source]." Zeitschrift Fur Allgemeine Mikrobiologie, vol. 23, no. 2, 1983, pp. 75-80.
Franke-Rinker D, Behrens U, Nöckel E. [Enzymatic study of citrate-isocitrate accumulation in yeast with glucose as the carbon source]. Z Allg Mikrobiol. 1983;23(2):75-80.
Franke-Rinker, D., Behrens, U., & Nöckel, E. (1983). [Enzymatic study of citrate-isocitrate accumulation in yeast with glucose as the carbon source]. Zeitschrift Fur Allgemeine Mikrobiologie, 23(2), 75-80.
Franke-Rinker D, Behrens U, Nöckel E. [Enzymatic Study of Citrate-isocitrate Accumulation in Yeast With Glucose as the Carbon Source]. Z Allg Mikrobiol. 1983;23(2):75-80. PubMed PMID: 6868652.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Enzymatic study of citrate-isocitrate accumulation in yeast with glucose as the carbon source]. AU - Franke-Rinker,D, AU - Behrens,U, AU - Nöckel,E, PY - 1983/1/1/pubmed PY - 1983/1/1/medline PY - 1983/1/1/entrez SP - 75 EP - 80 JF - Zeitschrift fur allgemeine Mikrobiologie JO - Z Allg Mikrobiol VL - 23 IS - 2 N2 - The connection between the kinetics of citrate-isocitrate overproduction by Saccharomycopsis lipolytica in glucose media and the specific activities of the enzymes being related to overproduction has been investigated. The specific activities of citrate synthase, aconitate hydratase, NAD+-linked and NADP+-linked isocitrate dehydrogenase decline significantly after exhaustion of the nitrogen source, whereas the activity of the pyruvate carboxylase remains relatively constant and corresponds to changes of the production rate. The results are compared with those obtained by fermentations in n-alkane media and discussed in relation to mechanisms of overproduction. SN - 0044-2208 UR - https://www.unboundmedicine.com/medline/citation/6868652/[Enzymatic_study_of_citrate_isocitrate_accumulation_in_yeast_with_glucose_as_the_carbon_source]_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0044-2208&date=1983&volume=23&issue=2&spage=75 DB - PRIME DP - Unbound Medicine ER -