BIOMAT Database Logo BIOMAT Database Logo

Metabolism of NAD+ in nuclei of Saccharomyces cerevisiae during stimulation of its biosynthesis by nicotinamide. 2001

T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Institute of Microbiology, Uzbekistan Academy of Sciences, ul. Abdully Kodiry 7B, Tashkent, 700128 Uzbekistan. imbasru@uzsci.net

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+-pyrophosphorylase, and NAD+ase activities.

UI MeSH Term Description Entries
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009536 Niacinamide An important compound functioning as a component of the coenzyme NAD. Its primary significance is in the prevention and/or cure of blacktongue and PELLAGRA. Most animals cannot manufacture this compound in amounts sufficient to prevent nutritional deficiency and it therefore must be supplemented through dietary intake. Nicotinamide,Vitamin B 3,Vitamin PP,3-Pyridinecarboxamide,Enduramide,Nicobion,Nicotinsäureamid Jenapharm,Papulex,Vitamin B3,3 Pyridinecarboxamide,B 3, Vitamin,B3, Vitamin,Jenapharm, Nicotinsäureamid
D011065 Poly(ADP-ribose) Polymerases Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE. ADP-Ribosyltransferase (Polymerizing),Poly ADP Ribose Polymerase,Poly(ADP-Ribose) Synthase,Poly(ADP-ribose) Polymerase,PARP Polymerase,Poly ADP Ribose Transferase,Poly ADP-Ribose Synthase,Poly(ADP-Ribose) Transferase,Poly(ADPR) Polymerase,Poly(ADPribose) Polymerase,Poly ADP Ribose Synthase,Polymerase, PARP,Synthase, Poly ADP-Ribose
D011755 Pyrophosphatases A group of enzymes within the class EC 3.6.1.- that catalyze the hydrolysis of diphosphate bonds, chiefly in nucleoside di- and triphosphates. They may liberate either a mono- or diphosphate. EC 3.6.1.-. Pyrophosphatase
D002467 Cell Nucleus Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed) Cell Nuclei,Nuclei, Cell,Nucleus, Cell
D000246 Adenosine Diphosphate Ribose An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins. ADP Ribose,Adenosine Diphosphoribose,ADP-Ribose,ADPribose,Adenosine 5'-Diphosphoribose,5'-Diphosphoribose, Adenosine,Adenosine 5' Diphosphoribose,Diphosphate Ribose, Adenosine,Diphosphoribose, Adenosine,Ribose, ADP,Ribose, Adenosine Diphosphate
D012441 Saccharomyces cerevisiae A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement. Baker's Yeast,Brewer's Yeast,Candida robusta,S. cerevisiae,Saccharomyces capensis,Saccharomyces italicus,Saccharomyces oviformis,Saccharomyces uvarum var. melibiosus,Yeast, Baker's,Yeast, Brewer's,Baker Yeast,S cerevisiae,Baker's Yeasts,Yeast, Baker

Related Publications

T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae.
April 2002, FEBS letters,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae.
October 2003, Molecular and cellular biology,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Cross-talk in NAD+ metabolism: insights from Saccharomyces cerevisiae.
October 2019, Current genetics,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Quantitation of NAD+ biosynthesis from the salvage pathway in Saccharomyces cerevisiae.
July 2009, Yeast (Chichester, England),
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Thiamine biosynthesis in Saccharomyces cerevisiae is regulated by the NAD+-dependent histone deacetylase Hst1.
July 2010, Molecular and cellular biology,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Polyadenylate metabolism in the nuclei and cytoplasm of Saccharomyces cerevisiae.
July 1975, The Journal of biological chemistry,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Role of NAD-linked glutamate dehydrogenase in nitrogen metabolism in Saccharomyces cerevisiae.
September 1990, Journal of bacteriology,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Nicotinamide Adenine Dinucleotide (NAD+) Biosynthesis in the Regulation of Metabolism, Aging, and Neurodegeneration.
January 2021, Holistic nursing practice,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Regulation of NAD+ metabolism, signaling and compartmentalization in the yeast Saccharomyces cerevisiae.
November 2014, DNA repair,
T G Gulyamova, and D M Ruzieva, and S M Nasmetova, and M R Shakirzyanova, and A M Kerbalaeva
Genistein enhances NAD+ biosynthesis by upregulating nicotinamide phosphoribosyltransferase in adipocytes.
November 2023, The Journal of nutritional biochemistry,
Copied contents to your clipboard!