Results 151 to 160 of about 176,600 (181)

Effects of inhibitors of spermidine synthase and spermine synthase on polyamine synthesis in rat tissues

Biochemical Pharmacology, 1993
Several inhibitors of aminopropyltransferases, developed recently in this laboratory, were tested for their specificity by measuring their effects on six enzyme activities related to polyamine biosynthesis and interconversion. Two of them, trans-4-methylcyclohexylamine (4MCHA) and N-(3-aminopropyl)cyclohexylamine (APCHA), selectively and potently ...
Keijiro Samejima, A Shirahata, K Samejima   +2 more
exaly   +3 more sources

Activation by spermine of citrate synthase from porcine heart

Biochimica Et Biophysica Acta - General Subjects, 1991
Spermine activated citrate synthase from porcine heart by decreasing the Km value for the substrate oxaloacetate without affecting the maximal velocity. Spermine markedly increased the maximal velocity of the saturation function with respect to acetyl-CoA as the substrate under conditions of intracellular concentrations of oxaloacetate, but the enzyme ...
Masataka Yoshino
exaly   +3 more sources

Spermine synthase in Snyder-Robinson syndrome and cancer

Molecular Biology Reports
Spermine synthase (Sms), a key enzyme in polyamine biosynthesis, catalyzes the conversion of spermidine to spermine using decarboxylated S-adenosylmethionine (dcAdoMet) as an aminopropyl donor. Although Sms is well-characterized in eukaryotes, it is relatively rare in bacteria, where spermine in some species is probably produced by non-specific ...
YERLİKAYA, AZMİ
openaire   +3 more sources

Spermine synthase activity affects the content of decarboxylated S-adenosylmethionine

Biochemical Journal, 2010
dcAdoMet (decarboxylated S-adenosylmethionine) is an essential intermediate in the synthesis of polyamines. Its content is normally very low, amounting to less than 5% of that of S-adenosylmethionine itself. It was found that in mice lacking spermine synthase there was a large increase in dcAdoMet and that overexpression of spermine synthase reduced ...
Anthony E, Pegg, Xiaojing, Wang, Charles E, Schwartz, Diane E, McCloskey   +3 more
openaire   +3 more sources

Spermine is not essential for growth of Saccharomyces cerevisiae: identification of the SPE4 gene (spermine synthase) and characterization of a spe4 deletion mutant

Gene, 1998
Spermine, ubiquitously present in most organisms, is the final product of the biosynthetic pathway for polyamines and is synthesized from spermidine. In order to investigate the physiological roles of spermine, we identified the SPE4 gene, which codes for spermine synthase, on the right arm of chromosome XII of Saccharomyces cerevisiae and prepared a ...
Yasuhiro Katagiri, Herbert Tabor, Celia White Tabor   +2 more
exaly   +3 more sources

Characterization of spermidine synthase and spermine synthase – The polyamine-synthetic enzymes that induce early flowering in Gentiana triflora

Biochemical and Biophysical Research Communications, 2015
Polyamines are essential for several living processes in plants. However, regulatory mechanisms of polyamines in herbaceous perennial are almost unknown. Here, we identified homologs of two Arabidopsis polyamine-synthetic enzymes, spermidine synthase (SPDS) and spermine synthase (SPMS) denoted as GtSPDS and GtSPMS, from the gentian plant, Gentiana ...
Keisuke Tasaki, Hideyuki Takahashi, Tomohiro Imamura   +2 more
exaly   +3 more sources

Molecular Cloning of a cDNA Encoding Human Spermine Synthase

DNA and Cell Biology, 1995
We have isolated and sequenced cDNA clones that encode human spermine synthase (EC 2.5.1.22). The total length of the sequenced cDNA was 1,612 nucleotides, containing an open reading frame encoding a polypeptide chain of 368 amino acids. All of the previously sequenced peptide fragments of human and bovine spermine synthase proteins could be located ...
V P, Korhonen, M, Halmekytö, L, Kauppinen, S, Myöhänen, J, Wahlfors, T, Keinänen, T, Hyvönen, L, Alhonen, T, Eloranta, J, Jänne   +9 more
openaire   +2 more sources

Use of (Gyro) Gy and Spermine Synthase Transgenic Mice to Study Functions of Spermine

2011
The polyamines putrescine, spermidine, and spermine are essential for mammalian cell growth, -differentiation, and cell death and have important physiological roles in all tissues. Many of the properties of polyamines that can be demonstrated in vitro are common to all three molecules with differences only in potency.
Xiaojing, Wang, Anthony E, Pegg
openaire   +2 more sources

Partial purification and characterization of spermine synthase from rat brain

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract Spermine synthase, the enzyme catalyzing the formation of spermine from spermidine and 5′-ndeoxy-5′- S -(3-methylthiopropylamine)sulphonium adenosine (decarboxylated S -adenosylmethionine) has been purified more than 100-fold from rat brain cytosol fraction.
P, Hannonen, J, Jänne, A, Raina
openaire   +2 more sources

Polyamine-linked sepharoses: Preparation and application to mammalian spermine synthase

Protein Expression and Purification, 1991
Seven different polyamine-linked Sepharose derivatives were prepared for the affinity chromatography of spermidine and spermine binding macromolecules: Spermine synthase from rat and hog brain was used as a model protein with a spermidine binding site.
A, Shirahata, C L, Zhu, S, Akatsu, Y, Suzuki, K, Samejima   +4 more
openaire   +2 more sources