Comparison of S-adenosylmethionine decarboxylases from rat liver and muscle

Pösö, Hannu; Pegg, Anthony E.

doi:10.1021/bi00256a013

Cited by 48 publications

(16 citation statements)

References 30 publications

(58 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although the mechanism by which MGBG brings about a marked decrease in Spd content (Fig. 8A) has not yet been determined, the compound may inhibit the activity of S-adenosylmethionine decarboxylase in the aleurone layers as it does in animal tissues (27,29,30). Inhibition of the decarboxylase activity wouid reduce the amount of decarboxylated form of Sadenosylmethionine available for the conversion of Put --Spd --Spm and thus result in decreased levels of Spd and Spm with increased level of Put in the aleurone layers (Fig.…”

Section: Methodsmentioning

confidence: 99%

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

Lin¹

1984

Plant Physiol.

View full text Add to dashboard Cite

ABSTRACrPolyamine metabolism and its relation to the induction of a-amylase formation in the aleurone layers of barley seeds (Hordeum vulgare cv Himalaya) in response to gibberellic acid (GA3) has been investipted. A high-performance liquid chromatographic system has been employed for qualitative and quantitative analyses of putrescine (Put), cadaverine (Cad), spermidine (Spd), spermine (Spm), and agmatine (Agm).Active polyamine metabolism occurs in the aleurone cells of deembryonate barley half seeds during imbibition. The aleurone layers isolated from fully imbibed half seeds contain about 880 nanomoles of Put, 920 nanomoles of Spd, and 610 nanomoles of Spm as free form per gram tissue dry weight while the levels of Cad and Agm are relatively low. The polyamine levels do not change significantly in the aleurone layers in response to added GA3 (1.5 micromolar) during the 8-hour lag period of the growth substance-induced formation of a-amylase. Also, the polyamine levels are not altered by the presence of abscisic acid (3 micromolar) which inhibits the enzyme induction by GA3. Kinetic studies show that both applied IU-"Cqornithine and lU-'4Carginine are primarily incorporated into Put during 2 hours of incubation, but the incorporation is not significantly affected by added GA3. Additionally, added GA3 does not affect the uptake and turnover of 11, nor research (18,37,38). Experiments with the aleurone layers of barley seeds have shown a number of biochemical events related to the synthesis of a-amylase in response to added GA3. The mass synthesis of a-amylase begins 8 to 10 h after exposure of the tissue to the growth substance (9). Syntheses and accumulation of a-amylase mRNA (17) and ER (38) start as early as 2 to 4 h after treatment of the growth substance. For efficient expression of a-amylase gene(s), it has recently been suggested that a newly synthesized protein is required (26). If GA3 has effects on translation, the synthesis ofthe unidentified protein factor could occur shortly after addition of the growth substance. Thus, it would be interesting to investigate possible biochemical changes within 2 h after exposure of the aleurone layers to GA3, and to determine whether any changes are related to the effects of the growth substance on the transcriptional and/or translational events described.The diamine Put2 and polyamines Spd and Spm are ubiquitous in biological materials (1, 33,35 (1,12,32,36). Several lines of evidence indicate that polyamines may be involved in regulation of structure, function, and/or biosynthesis ofmacromolecules (10,16,24,28). In higher plants, polyamine metabolism has been related to the action of plant growth substances on regulation of plant growth and development (7, 8, 13, 22). In the internodes of light-grown dwarf peas the contents of Put and Spd per internode have been shown to increase during the elongation induced by exogenously applied GA3 (13). Also, it has been reported that the addition of GA3 results in 4-fold increase in the activity ofornithine decarboxyla...

show abstract

Section: Methodsmentioning

confidence: 99%

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

Lin¹

1984

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…Crude ADCs from rat liver (Poso & Pegg, 1982), yeast (P6so et al, 1975b) and Pseudomonas aeruginosa (P6so et al, 1976) were prepared by published methods cited. Highly purified rat liver ADC was prepared as described by Poso & Pegg (1982).…”

Section: Sources Of Adenosylmethionine Decarboxylasesmentioning

confidence: 99%

“…Highly purified rat liver ADC was prepared as described by Poso & Pegg (1982). The specific activity of the final preparation of ADC was more than 500 units/mg of protein (Poso & Pegg, 1982) and the preparation gave a single band when analysed by polyacrylamide-gel electrophoresis under denaturing conditions as described by Pos6 & Pegg (1982). About 0.03 unit was used in each assay.…”

Section: Sources Of Adenosylmethionine Decarboxylasesmentioning

confidence: 99%

Irreversible inhibition of putrescine-stimulated S-adenosyl-l-methionine decarboxylase by berenil and pentamidine

Karvonen¹,

Kauppinen²,

Partanen³

et al. 1985

Biochemical Journal

View full text Add to dashboard Cite

The putrescine-stimulated S-adenosyl-L-methionine decarboxylases from rat liver and yeast were strongly inhibited by Berenil and to a lesser extent by Pentamidine. Ten times greater drug concentrations were needed to achieve a similar level of inhibition of a Mg2+-stimulated bacterial enzyme. The inhibition was irreversible in that extensive dialyses or precipitation with (NH4)2SO4 did not restore enzyme activity. Putrescine did not protect the enzyme against Berenil, but adenosylmethionine either alone or with putrescine partially protected the irreversible action of Berenil. The compound 4,4′-diamidinodiphenylamine, which differs from Berenil only in lacking the azo group between benzene rings, was a weaker inhibitor than Berenil, and its inhibition was reversible. Berenil also inhibited the activity of adenosylmethionine decarboxylase in vivo, by depressing the activity of the enzyme in normal rat liver, for at least 24 h after a single injection (50 mg/kg body wt.) of the drug.

show abstract

“…10-fold lower than those reported for the E. coli and rat enzymes at their physiological temperatures; the even lower specific activity of the S. solfataricus preparation may reflect the difficulty in purifying this low-abundance protein from its native source. MGBG competitively inhibits the M. jannaschii enzyme with affinity comparable to that for the E. coli enzyme; both the E. coli and M. jannaschii enzymes have lower affinity for MGBG than do the mammalian enzymes (24).…”

Section: Resultsmentioning

confidence: 94%

“…MGBG is a general inhibitor of AdoMetDCs, although it has higher affinity for the eucaryotic enzymes (21). Immobilized MGBG has been used to purify eucaryotic and E. coli AdoMetDCs (4,8,14,21,24). Recombinant M. jannaschii AdoMetDC was purified from E. coli by affinity chromatography on MGBG-Sepharose and subsequent gel filtration as described in Materials and Methods.…”

Section: Resultsmentioning

confidence: 99%

S -Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii : Identification of a Novel Family of Pyruvoyl Enzymes

et al. 2000

View full text Add to dashboard Cite

Polyamines are present in high concentrations in archaea, yet little is known about their synthesis, except by extrapolation from bacterial and eucaryal systems. S-Adenosylmethionine (AdoMet) decarboxylase, a pyruvoyl group-containing enzyme that is required for spermidine biosynthesis, has been previously identified in eucarya and Escherichia coli. Despite spermidine concentrations in the Methanococcales that are several times higher than in E. coli, no AdoMet decarboxylase gene was recognized in the complete genome sequence of Methanococcus jannaschii. The gene encoding AdoMet decarboxylase in this archaeon is identified herein as a highly diverged homolog of the E. coli speD gene (less than 11% identity). The M. jannaschii enzyme has been expressed in E. coli and purified to homogeneity. Mass spectrometry showed that the enzyme is composed of two subunits of 61 and 63 residues that are derived from a common proenzyme; these proteins associate in an (␣␤) 2 complex. The pyruvoyl-containing subunit is less than one-half the size of that in previously reported AdoMet decarboxylases, but the holoenzyme has enzymatic activity comparable to that of other AdoMet decarboxylases. The sequence of the M. jannaschii enzyme is a prototype of a class of AdoMet decarboxylases that includes homologs in other archaea and diverse bacteria. The broad phylogenetic distribution of this group suggests that the canonical SpeD-type decarboxylase was derived from an archaeal enzyme within the gamma proteobacterial lineage. Both SpeD-type and archaeal-type enzymes have diverged widely in sequence and size from analogous eucaryal enzymes.Polyamines are ubiquitous small molecules that are found at high concentrations in most organisms (7,16,30). They appear to stabilize molecular complexes, such as ribosomes, and to facilitate protein-nucleic acid interactions. Deregulation or inhibition of polyamine synthesis broadly affects the eucaryal cell cycle, making these enzymes attractive targets for drug therapy against cancer and parasitic infections (15).Mesophilic species of the Methanococcales group of methanogenic euryarchaea contain substantial concentrations of three common polyamines: putrescine (0.5 to 3.4 mol/g), 1,3-diaminopropane (0.3 mol/g), and spermidine (29 to 40 mol/g) (27). Putrescine, the diamine precursor to spermidine, is produced either by the single enzyme ornithine decarboxylase or by the consecutive actions of arginine decarboxylase and agmatine ureohydrolase. Spermidine synthase catalyzes the transfer of a propylamine moiety to putrescine, producing spermidine, a triamine.The most unusual feature of spermidine biosynthesis is the nature of the propylamine donor, decarboxylated S-adenosylmethionine (AdoMet) (35). AdoMet plays a central role in the metabolism of all known organisms (31). AdoMet is best known as an activated methyl donor used by cells to modify DNA, RNA, proteins, cofactors, lipids, etc. In addition, eucaryotes, some bacteria, and the crenarchaeon Sulfolobus solfataricus have been shown to contain AdoMet...

show abstract

Comparison of S-adenosylmethionine decarboxylases from rat liver and muscle

Cited by 48 publications

References 30 publications

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

Polyamine Metabolism and Its Relation to Response of the Aleurone Layers of Barley Seeds to Gibberellic Acid

Irreversible inhibition of putrescine-stimulated S-adenosyl-l-methionine decarboxylase by berenil and pentamidine

S -Adenosylmethionine Decarboxylase from the Archaeon Methanococcus jannaschii : Identification of a Novel Family of Pyruvoyl Enzymes

Contact Info

Product

Resources

About