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Gulyamova, T. G.; Ruzieva, D. M.; Nasmetova, S. M.; Shakirzyanova, M. R.; Kerbalaeva, A. M.

doi:10.1023/a:1012313408062

Biochemistry (Moscow)

2001

DOI: 10.1023/a:1012313408062

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T. G. Gulyamova

D. M. Ruzieva

S. M. Nasmetova

et al.

Abstract: The activities of nuclear enzymes involved in NAD+ metabolism in Saccharomyces cerevisiae strain 913a-1 and its mutant 110 previously selected as an NAD+ producer were investigated. The presence of extracellular nicotinamide increased the total NAD+ pool in the cells and increased [3H]nicotinic acid incorporation; however, NAD+ concentration in isolated nuclei decreased slightly. The stimulating effect of nicotinamide on intracellular synthesis of NAD+ correlated with increases in ADP-ribosyl transferase, NAD+… Show more

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“…Thus, based on the results, it can be confirmed that the increase in the intracellular NAD concentration in the local yeast strain S. cerevisiae 913a-1 that was observed by us earlier [7] is due to the presence of cytoplasmic proteins that possess enzymatic activity for transforming 3-MP into NA.…”

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Transformation of 3-methylpyridine into nicotinic acid by the yeast S. cerevisiae

et al. 2006

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It has been shown that the yeast S. cerevisiae has the ability to synthesize nicotinic acid and NAD from 3-methylpyridine. Fractionation of intracellular yeast proteins established that the fraction of molecular weight 65-90 kDa had the highest activity for transformation of pyridine derivatives into nicotinate. HPLC showed that, in addition to nicotinic acid, nicotinamide was also present in the intermediates during transformation of 3-methylpyridine. The results were consistent with the presence in yeast cells of an enzymatic system that transforms 3-methylpyridine into vitamin PP.Nicotinic acid (NA) is known to be produced chemically from the pyridine derivatives β-picoline (3-methylpyridine, 3-MP) or 3-acetylpyridine (3-AP) [1]. The question of NA production in microbiological conversions was first raised in the 1970s by researchers [2-4] who isolated more than 100 cultures of Mycobacterium, Nocardia, Corynebacterium, and Arthrobacter and others that not only decomposed the pyridine ring but also oxidized alkyl substituents on it without destroying it. Also, the ability to oxidize the methyl on 3-MP was first demonstrated at that time. However, the enzymatic aspects of the microbiological transformation of pyridine derivatives have been poorly studied despite the other successes.We observed previously that local strains of the yeast Saccharomyces cerevisiae 913a-1, which were selected as producers of nicotinamideadeninedinucleotide (NAD), accumulate high concentrations of the coenzyme in the presence of 3-MP and 3-AP [5]. This suggests that enzymatic transformation of these compounds into nicotinate and its subsequent participation in NAD biosynthesis is possible. Therefore, our goal was to find intracellular proteins that are involved in the bioconversion of 3-MP into NA by S. cerevisiae 913a-1.Fermentation of S. cerevisiae 913a-1 biomass in the presence of 3-MP is accompanied by more than a doubling of the intracellular NAD concentration (from 35.6 to 68.2 µg/mL) whereas the free NA content did not change (8.6 µg/mL).However, it should be considered that intracellular NA is an intermediate in many exchange transformations of pyridinenucleotides whereas the intracellular content of free NA is low compared with that of nicotinamide or NAD. Thus, the ability of yeast cells to accumulate high concentrations of NAD indicates that biosynthesis can supply the required amount of NA. The increased intracellular pool of NAD observed in yeast in the presence of 3-MP may be due to its preliminary transformation into nicotinate due to its enzymatic transformation in cytoplasm. According to the literature, various microorganism groups can not only completely degrade pyridine bases but also partially transform them. Thus, the ability of the bacteria Nocardia and Arthrobacter to oxidize under co-oxidation conditions alkylpyridines to the corresponding acids, 3-and 2-MP to nicotinic and picolinic acids, has been demonstrated. Transformation of pyridine into nicotinamide also occurs through NA or other intermediates such as ...

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Transformation of 3-methylpyridine into nicotinic acid by the yeast S. cerevisiae

et al. 2006

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Yeast (ADPribosyl)ation: Revisiting a controversial question

Faraone-Mennella

Maio

Petrella

et al. 2005

J of Cellular Biochemistry

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The controversy about the occurrence of an (ADPribosyl)ating activity in yeast is still standing up. Here we discuss this topic on the basis of results obtained with classic experiments proposed over years as basis to characterize an (ADPribosyl)ation system in any organism. Independent results obtained in two different laboratories were in line with each other and went towards the occurrence of an active (ADPribosyl)ating system in Saccharomyces cerevisiae. In fact data collected from nuclear preparations of cultured cells matched those from baker's yeast and lyophilized yeast cells. Yeast (ADPribosyl)ating enzyme is a protein of 80-90 kDa, as determined by electrophoresis on polyacrylamide gel in sodium dodecyl sulphate, followed by immunoblotting with antibodies against anti-poly(ADPribose) polymerase catalytic site. It synthesizes products, that, after digestion with phosphodiesterase, co-migrates mainly with phosphoribosyl adenosine monophosphate after thin layer chromatography on silica gel plate.

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Current Awareness

2002

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Books, Reviews & Symposia; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (3 weeks journals ‐ search completed 5th. Dec. 2001)

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Cited by 3 publications

References 8 publications

Transformation of 3-methylpyridine into nicotinic acid by the yeast S. cerevisiae

Transformation of 3-methylpyridine into nicotinic acid by the yeast S. cerevisiae

Yeast (ADPribosyl)ation: Revisiting a controversial question

Current Awareness

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