Nitrite reduction in Veillonella alcalescens
نویسندگان
چکیده
منابع مشابه
Ribose utilization by Veillonella alcalescens.
The utilization of ribose by Veillonella alcalescens has been further investigated. Nonfermentation of ribose is not a result of a phosphorylation lesion since ribose-phosphorylating activity was measured in cell extracts. Resting cells accumulated ribose-5-phosphate and nucleotides when (14)C-ribose was provided; no other sugar phosphates were detectable. Resting cells that were shifted to gro...
متن کاملNitrate reduction and the growth of Veillonella alcalescens.
Veillonella alcalescens, a strict anaerobe, was found to possess a nitrate reductase system which has characteristics of both assimilatory and respiratory nitrate reduction. The nitrate reductase has been identified tentatively as a particulate enzyme which utilizes a variety of electron donors for the reduction of nitrate. By use of (15)N-labeled nitrate, it was shown that under appropriate co...
متن کاملKinetic properties of phosphotransacetylase from Veillonella alcalescens.
The phosphotransacetylase of Veillonella alcalescens catalyzes a reversible reaction with Michaelis-Menten kinetics for all substrates. The rate of the reverse reaction (the synthesis of acetyl coenzyme A from acetyl phosphate) was 6.5 times greater than the rate of the forward reaction (the synthesis of acetyl phosphate from acetyl coenzyme A). The apparent K(m) values determined for the forwa...
متن کاملSuccinic Acid Degradation by Veillonella Alcalescens.
samples were thus obtained for subsequent anaerobic assay with P. cereviseae. Typical assay results are indicated in Fig. 2. There is a marked increase in P. cereviseae activity caused by incubation of C. sporogenes with folic acid as compared with the corresponding nonincubated system. This activity could not be attributed to endogenous cell activity, and was not due to the utilization of aryl...
متن کاملRegulatory properties of acetokinase from Veillonella alcalescens.
Acetokinase from Veillonella alcalescens catalyzes the virtually irreversible synthesis of adenosine triphosphate from acetyl phosphate and adenosine diphosphate. Kinetic analysis revealed that the enzyme was activated by acetyl phosphate and inhibited by adenosine triphosphate. Velocity curves obtained with increasing amounts of adenosine diphosphate were of the Michaelis-Menten type (rectangu...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1979
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.137.2.905-911.1979