Metabolism and Degradation of Nicotinic Acid in Parsley (Petroselinum hortense) Cell Suspension Cultures and Seedlings

1986 ◽  
Vol 41 (1-2) ◽  
pp. 148-157 ◽  
Author(s):  
Ludger Schwenen ◽  
Dieter Komoßa ◽  
Wolfgang Barz

Abstract Application of [6-14C]-or [7-14C]nicotinic acid to parsley cell suspension cultures led to the accumulation of labelled nicotinamide mononucleotide, nicotinamide adenine dinucleotide, nicotinamide N-riboside, nicotinamide and nicotinic acid, indicating the operation of the pyridine nucleotide cycle in these cells. As main conjugates, nicotinic acid N-glucoside and nicotinic acid glucose ester were found. For nicotinic acid degradation the following sequence is suggested: nicotinic acid → 6-hydroxynicotinic acid → 2,5-dihydroxypyridine → a C4/C3 unit of unknown structure → CO2. In aseptically grown parsley seedlings nicotinic acid is also degraded to CO2

1988 ◽  
Vol 43 (11-12) ◽  
pp. 843-849 ◽  
Author(s):  
Dieter Komoßa ◽  
Wolfgang Barz

Abstract A degradation product of nicotinic acid representing the pyridine carbon skeleton was isolated and purified from parsley cell suspension cultures after incubation with [6-14C]nicotinic acid for 70 h. The catabolite was identified as glutaric acid by means of spectroscopic (GC-MS and 1H NMR) and chromatographic (TLC, HPLC) techniques. Glutaric acid when applied to parsley cell cultures was readily degraded to CO2 but intermediate products could not be identified.


1988 ◽  
Vol 43 (11-12) ◽  
pp. 835-842 ◽  
Author(s):  
Barbara Upmeier ◽  
Jürgen E. Thomzik ◽  
Wolfgang Barz

Abstract A soluble enzyme catalyzing the transfer of the glucose moiety from UDP-glucose to the nitrogen atom of nicotinic acid was detected in protein preparations from heterotrophic cell suspension cultures of parsley (Petroselinum hortense Hoffm.). Enzyme activity was enriched 22-fold by ammonium sulfate precipitation, gel filtration and ion exchange chromatography. The UDP-glucose : nicotinic acid-N-glucosyltransferase showed a pH-optimum at pH 7.8-8.2 and a temperature optimum at 30 °C. The apparent KM values were determined to be 170 μM for nicotinic acid and 1.2 mM for the cosubstrate. The native enzyme had a molecular mass of about 46 kDa. The glucosyltransferase reaction was shown to be reversible. The transfer of the glucose molecule from nicotinic acid-N-glucoside to uridinediphosphate yielding uridinediphosphoglucose and nicotinic acid could be demonstrated indicating that nicotinic acid-N-glucoside has a high group-transfer potential.


1976 ◽  
Vol 54 (24) ◽  
pp. 2924-2927 ◽  
Author(s):  
Donald K. Dougall ◽  
Jeff Bloch

Evidence was sought for the presence of glutamate synthase (EC 2.6.1.53) in extracts from suspension cultures of six higher plant species not previously examined. The level of glutamate synthase measured was above the level of glutamic dehydrogenase (EC 1.4.1.2, 1.4.1.4) in extracts of soybean, parsley, okra, and cotton. Glutamate synthase was detectable but less than glutamic dehydrogenase in extracts of sugarcane. Glutamate synthase was not detected in extracts of peanut. Evidence for two glutamate synthases, each specific for one pyridine nucleotide, was obtained with cultures of carrot. Glutamate synthase has now been detected in eight and possibly nine species representing four and possibly five families of higher plants.


1988 ◽  
Vol 27 (11) ◽  
pp. 3489-3493 ◽  
Author(s):  
Barbara Upmeier ◽  
Jürgen E. Thomzik ◽  
Wolfgang Barz

Sign in / Sign up

Export Citation Format

Share Document