Glutamate Biosynthesis in Anaerobic Bacteria. II. Stereospecificity of Aconitase and Citrate Synthetase of Clostridium kluyveri*

Biochemistry ◽  
1966 ◽  
Vol 5 (4) ◽  
pp. 1119-1124 ◽  
Author(s):  
Joseph R. Stern ◽  
C. S. Hegre ◽  
Gunta Bambers
Keyword(s):  
Anaerobic Bacteria ◽  
Clostridium Kluyveri ◽  
Glutamate Biosynthesis ◽  
Citrate Synthetase

scholarly journals Ultrastructure of the Obligately Anaerobic Bacteria Clostridium Kluyveri and Cl. Acetobutylicum

1973 ◽  
Vol 26 (3) ◽  
pp. 547 ◽  
Author(s):  
KY Cho ◽  
CH Doy
Keyword(s):  
Cell Wall ◽  
Anaerobic Bacteria ◽  
Total Thickness ◽  
Obligately Anaerobic ◽  
Number Of Layers ◽  
Clostridium Kluyveri

The morphology of Cl. kluyveri is compared with that of CI. acetobutylicum. The multilayered cell wall of both organisms differ in the number of layers and total thickness.

Confirmation of unusual stereochemistry of glutamate biosynthesis in clostridium kluyveri

FEBS Letters ◽  
1968 ◽  
Vol 1 (1) ◽  
pp. 74-76 ◽  
Author(s):  
Kurt Jungermann ◽  
Rudolf K. Thauer ◽  
Joseph Wenning ◽  
Karl Decker
Keyword(s):  
Clostridium Kluyveri ◽  
Glutamate Biosynthesis

scholarly journals Re-Citrate Synthase from Clostridium kluyveri Is Phylogenetically Related to Homocitrate Synthase and Isopropylmalate Synthase Rather Than to Si-Citrate Synthase

2007 ◽  
Vol 189 (11) ◽  
pp. 4299-4304 ◽  
Author(s):  
Fuli Li ◽  
Christoph H. Hagemeier ◽  
Henning Seedorf ◽  
Gerhard Gottschalk ◽  
Rudolf K. Thauer
Keyword(s):  
Primary Structure ◽  
Coenzyme A ◽  
Citrate Synthase ◽  
Anaerobic Bacteria ◽  
Strictly Anaerobic ◽  
Acetyl Coenzyme A ◽  
Isopropylmalate Synthase ◽  
Cell Extracts ◽  
Homocitrate Synthase ◽  
Clostridium Kluyveri

ABSTRACT The synthesis of citrate from acetyl-coenzyme A and oxaloacetate is catalyzed in most organisms by a Si-citrate synthase, which is Si-face stereospecific with respect to C-2 of oxaloacetate. However, in Clostridium kluyveri and some other strictly anaerobic bacteria, the reaction is catalyzed by a Re-citrate synthase, whose primary structure has remained elusive. We report here that Re-citrate synthase from C. kluyveri is the product of a gene predicted to encode isopropylmalate synthase. C. kluyveri is also shown to contain a gene for Si-citrate synthase, which explains why cell extracts of the organism always exhibit some Si-citrate synthase activity.

Glutamate Biosynthesis in Lactococcus lactis subsp. lactis NCDO 2118

1998 ◽  
Vol 64 (7) ◽  
pp. 2485-2489 ◽  
Author(s):  
P. Lapujade ◽  
M. Cocaign-Bousquet ◽  
P. Loubiere
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Lactococcus Lactis ◽  
Anaerobic Bacteria ◽  
Glutamate Synthase ◽  
Lag Phase ◽  
Carboxylase Activity ◽  
Nitrogen Donor ◽  
Reference Medium ◽  
Glutamate Biosynthesis

ABSTRACT Unlike other lactic acid bacteria, Lactococcus lactissubsp. lactis NCDO 2118 was able to grow in a medium lacking glutamate and the amino acids of the glutamate family. Growth in such a medium proceeded after a lag phase of about 2 days and with a reduced growth rate (0.11 h−1) compared to that in the reference medium containing glutamate (0.16 h−1). The enzymatic studies showed that a phosphoenolpyruvate carboxylase activity was present, while the malic enzyme and the enzymes of the glyoxylic shunt were not detected. As in most anaerobic bacteria, no α-ketoglutarate dehydrogenase activity could be detected, and the citric acid cycle was restricted to a reductive pathway leading to succinate formation and an oxidative branch enabling the synthesis of α-ketoglutarate. The metabolic bottleneck responsible for the limited growth rate was located in this latter pathway. As regards the synthesis of glutamate from α-ketoglutarate, no glutamate dehydrogenase was detected. While the glutamate synthase-glutamine synthetase system was detected at a low level, high transaminase activity was measured. The conversion of α-ketoglutarate to glutamate by the transaminase, the reverse of the normal physiological direction, operated with different amino acids as nitrogen donor. All of the enzymes assayed were shown to be constitutive.

Application of commercial test-systems to identify gram-negative facultatively anaerobic bacteria

2016 ◽  
Vol 3 (1) ◽  
pp. 43-48 ◽  
Author(s):  
V. Patyka ◽  
L. Butsenko ◽  
L. Pasichnyk
Keyword(s):  
Erwinia Amylovora ◽  
Anaerobic Bacteria ◽  
Biochemical Properties ◽  
Test System ◽  
Phytopathogenic Bacteria ◽  
Gram Negative ◽  
Test Systems ◽  
Facultatively Anaerobic ◽  
Microbiological Methods

Aim. To validate the suitability of commercial API 20E test-system (bioMerieux) for the identifi cation and characterization of facultative gram-negative phytopathogenic bacterial isolates. Methods. Conventional mi- crobiological methods, API 20E test-system (bioMerieux) according to the manufacturer’s instructions. Re- sults. The identifi cation results for Erwinia amylovora, Pectobacterium carotovorum and Pantoea agglome- rans isolates were derived from the conventional and API 20E test systems, which, were in line with the literature data for these species. The API 20E test-system showed high suitability for P. agglomerans isolates identifi cation. Although not all the species of facultatively anaerobic phytopathogenic bacteria may be identi- fi ed using API 20E test-system, its application will surely allow obtaining reliable data about their physiologi- cal and biochemical properties, valuable for identifi cation of bacteria, in the course of 24 h. Conclusions. The results of tests, obtained for investigated species while using API 20E test-system, and those of conventional microbiological methods coincided. The application of API 20E test-system (bioMerieux) ensures fast obtain- ing of important data, which may be used to identify phytopathogenic bacteria of Erwinia, Pectobacterium, Pantoea genera.

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