Results 91 to 100 of about 241 (129)

Juglorin, a new spermidine synthase inhibitor.

open access: yesThe Journal of Antibiotics, 1987
K, Hamaguchi   +5 more
openaire   +3 more sources

Helicobacter pylori does not use spermidine synthase to produce spermidine

Biochemical and Biophysical Research Communications, 2017
Helicobacter pylori is the primary pathogen associated to gastritis and gastric cancer. Growth of H. pylori depends on the availability of spermidine in vivo. Interestingly, the genome of H. pylori contains an incomplete set of genes for the classical pathway of spermidine biosynthesis.
Shannon Wing Ngor Au, Huawei Zhang
exaly   +3 more sources

Nucleotide Sequence of Mouse Spermidine Synthase cDNA

DNA Sequence, 1994
The nucleotide sequence of mouse cDNA for spermidine synthase appeared to contain 75 nucleotides of 5' untranslated region, an open reading frame of 909 nucleotides and 297 nucleotides of 3' untranslated region. The open reading frame encoded a polypeptide of 302 amino acids, displaying 95% similarity to human and 33% similarity to E.
Leena Alhonen   +2 more
exaly   +3 more sources

Characterization of spermidine synthase from Trypanosoma brucei brucei

Molecular and Biochemical Parasitology, 1984
Spermidine synthase from Trypanosoma brucei brucei was characterized and found to be similar to spermidine synthase from other sources. The Km for putrescine was found to be 0.2 mM and the Km for decarboxylated S-adenosylmethionine 0.1 microM. The approximate molecular weight of the enzyme was 74 000 as determined by a combination of molecular sieve ...
A J Bitonti, Peter P McCann, P P McCann
exaly   +3 more sources

Androgen regulation of spermidine synthase expression in the rat prostate

Prostate, 2002
AbstractBACKGROUNDSpermidine synthase, an essential enzyme in the polyamine synthesis pathway, was identified as one of the androgen‐response genes in the rat ventral prostate. Characterization of androgen regulation of spermidine synthase is important to the understanding of androgenic regulation of polyamine synthesis.METHODSFull‐length cDNA encoding
Zhou Wang
exaly   +3 more sources

Genetic analysis of spermidine synthase from Leishmania donovani

Molecular and Biochemical Parasitology, 2001
The polyamine biosynthetic pathway of protozoan parasites has been validated as a target in antiparasitic chemotherapy. To investigate this pathway at the biochemical and genetic level in a model parasite, the gene encoding spermidine synthase (SPDSYN), a key polyamine biosynthetic enzyme, has been cloned and sequenced from Leishmania donovani.
Sigrid Roberts   +2 more
exaly   +3 more sources

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   +2 more
exaly   +3 more sources

Structure and Mechanism of Spermidine Synthases

Biochemistry, 2007
Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers ...
Hong, Wu   +7 more
openaire   +2 more sources

Immunolocalisation of spermidine synthase in Solanum tuberosum

Phytochemistry, 2013
Spermidine synthase (SPDS) catalyses the formation of spermidine, which is an essential polyamine and widespread in living organisms. Spermidine is formed from putrescine by transfer of an aminopropyl group from decarboxylated S-adenosylmethionine. Spermidine is also a precursor to further polyamines, such as spermine and thermospermine, most of which ...
Yvonne, Sichhart, Birgit, Dräger
openaire   +2 more sources

Putrescine derivatives as substrates of spermidine synthase

International Journal of Biochemistry, 1987
1. Derivatives of 1,4-butanediamine (putrescine) were studied in vitro and in vivo as potential substrates of spermidine synthase. 2. Substituents in the 1-position decreased the reaction rate by steric hindrance, and in the case of electron withdrawing groups there was an additional decrease due to the lowered basicity of the vicinal amino group.
S, Sarhan, F, Dezeure, N, Seiler
openaire   +2 more sources

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