Biosynthesis of dolichol phosphate by subcellular fractions from liver

Daleo, Gustavo Raúl; Hopp, H. Esteban; Romero, Pedro; Lezica, Rafael Pont

doi:10.1016/0014-5793(77)80566-8

Cited by 51 publications

(14 citation statements)

References 18 publications

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“…cis-Prenyltransferase (dehydrodolichyl diphosphate synthase; cis-PT) is a key enzyme in dolichol synthesis and represents the first enzyme of the polyprenyl branch of the mevalonate pathway. The enzyme catalyzes the elongation of the polyprenol chain by sequential addition of IPP to farnesyl diphosphate (485)(486)(487). Polyprenyl diphosphate formed in this reaction is then dephosphorylated by isoprenoid phosphatase, the ␣-prenyl residue is saturated, and the resultant dolichol can be installed in the structure of cell membranes.…”

Section: Synthesis Of Farnesyl Diphosphate (Fpp) (I) Acetoacetyl-coamentioning

confidence: 99%

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll

Dattenböck

Carreras-Villaseñor

et al. 2016

Microbiol Mol Biol Rev

166

195

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SUMMARYThe genusTrichodermacontains fungi with high relevance for humans, with applications in enzyme production for plant cell wall degradation and use in biocontrol. Here, we provide a broad, comprehensive overview of the genomic content of these species for “hot topic” research aspects, including CAZymes, transport, transcription factors, and development, along with a detailed analysis and annotation of less-studied topics, such as signal transduction, genome integrity, chromatin, photobiology, or lipid, sulfur, and nitrogen metabolism inT. reesei,T. atroviride, andT. virens, and we open up new perspectives to those topics discussed previously. In total, we covered more than 2,000 of the predicted 9,000 to 11,000 genes of eachTrichodermaspecies discussed, which is >20% of the respective gene content. Additionally, we considered available transcriptome data for the annotated genes. Highlights of our analyses include overall carbohydrate cleavage preferences due to the different genomic contents and regulation of the respective genes. We found light regulation of many sulfur metabolic genes. Additionally, a new Golgi 1,2-mannosidase likely involved inN-linked glycosylation was detected, as were indications for the ability ofTrichodermaspp. to generate hybrid galactose-containingN-linked glycans. The genomic inventory of effector proteins revealed numerous compounds unique toTrichoderma, and these warrant further investigation. We found interesting expansions in theTrichodermagenus in several signaling pathways, such as G-protein-coupled receptors, RAS GTPases, and casein kinases. A particularly interesting feature absolutely unique toT. atrovirideis the duplication of the alternative sulfur amino acid synthesis pathway.

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Section: Synthesis Of Farnesyl Diphosphate (Fpp) (I) Acetoacetyl-coamentioning

confidence: 99%

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Schmoll

Dattenböck

Carreras-Villaseñor

et al. 2016

Microbiol Mol Biol Rev

166

195

View full text Add to dashboard Cite

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“…Cis-prenyltransferase (dehydrodolichyl diphosphate synthase) (cis-PT), a key enzyme in dolichol synthesis, is the Wrst enzyme of the polyprenol branch of the mevalonate pathway. The enzyme catalyzes the elongation of polyprenol chain by sequential addition of isopentenyl diphosphate (IPP) to farnesyl diphosphate (FPP) (Adair and Cafmeyer, 1987;Daleo et al, 1977;Szkopijska et al, 1996). In the yeast S. cerevisiae cis-PT is encoded by two genes RER2 and SRT1 (Sato et al, 2001;Shenk et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Perlińska-Lenart¹,

Bańkowska²,

Palamarczyk³

et al. 2006

Fungal Genetics and Biology

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“…Given that dolichol is synthesized de now as Dol-P-P [34,35] and that it also appears as a final product in the biosynthetic glycoprotein cycle, it is clear that the existence of Dol-P-P phosphatase is essential to the starting and reinitiation of the cycle. On the other hand, the existence of free dolichol in many tissues [36] indicates that in addition to Dol-P-P phosphatase, Dol-P phosphatase must also be present.…”

Section: Ejjccts Of Phosphorylated Compoundsmentioning

confidence: 99%

Dolichyl‐Phosphate Phosphatase and Dolichyl‐Diphosphate Phosphatase in Rat‐Liver Microsomes

Belocopitow

Boscoboinik

1982

European Journal of Biochemistry

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Dolichyl-phosphate phosphatase and dolichyl-diphosphate phosphatase activities of a liver-cell microsomal preparation were solubilized by treatment with Triton X-100. The I00000 x g supernatant was then passed through a column of Sepharose-4B -concanavalin A. Both enzyme activities were found in the percolate. This treatment eliminated inhibition by ATP and glucose 6-phosphate in both phosphatase activities. In each case the activities were inhibited by higher concentrations of enzyme preparation due to the presence of phospholipids. The inhibitory effects of either phosphatidylcholine or phosphatidylethanolamine were due to competition for detergent. On the other hand, the effect produced by phosphatidic acid appeared to be different, since it did not change the optimal concentration of Triton X-100 for the two enzymes. Dolichyl-phosphate phosphatase was strongly inhibited by both Pi and PPi, whereas dolichyl-diphosphate phosphatase was only slightly inhibited by Pi and not at all by PPi. Dolichyl-diphosphate phosphatase was more inhibited by divalent cations than dolichyl-phosphate phosphatase. The apparent K,,, of dolichyl-phosphate phosphatase for dolichyl phosphate was 0.15 mM. Dolichol also inhibited dolichyl-phosphate phosphatase, but it produced a stronger inhibition on dolichyl-diphosphate phosphatase. The inhibitory effect of dolichol was not entirely due to detergent competition.The enzymatic system involved in the biosynthesis of asparagine-linked glycoproteins is located in the endoplasmic reticulum. In this biosynthetic process the formation of the peptide linkage precedes the formation of the covalent bond between oligosaccharide and amino acid. During the last decade experimental evidence has shown that, at least in the case of asparagine-type glycoproteins, the oligosaccharide moiety is built up linked to dolichol diphosphate. The Dol-P-P moiety is released when to oligosaccharide moiety is transferred to the peptide chain [1,2]. Since the biosynthesis of the oligosaccharide lipid is initiated with dolichyl monophosphate as an acceptor of the first glycosyl groups, it seems reasonable to assume the existence of a conversion step from Dol-P-P to Dol-P, which would complete the cycle.Some suggestions [3] and further experimental evidence [4-71 indicate that an increased concentration of dolichyl phosphate would in turn increase the rate of glycoprotein synthesis. The Dol-P concentration would be determined by the activity of the following three enzymes.a) The enzyme that forms Dol-P from dolichol, dolichol phosphokinase [8-111, which catalyzes the reaction Dolichol + CTP -+ Dol-P + CDP .b) The enzyme that forms Dol-P by a cleavage of the pyrophosphate bond of Dol-P-P, Dol-P-P phosphatase [I2 -141. The reaction is Dol-P-P + Dol-P + Pi.c) The enzyme that lowers Dol-P concentration through a transformation of the latter into dolichol, Dol-P phosphatase [12,13,15,16].Abbreviations. Dol-P-P, dolichyl diphosphate; Dol-P, dolichyl phosphate.In the studies reported below we have focused on the characteri...

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Biosynthesis of dolichol phosphate by subcellular fractions from liver

Cited by 51 publications

References 18 publications

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

The Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species

Overexpression of the Saccharomyces cerevisiae RER2 gene in Trichoderma reesei affects dolichol dependent enzymes and protein glycosylation

Dolichyl‐Phosphate Phosphatase and Dolichyl‐Diphosphate Phosphatase in Rat‐Liver Microsomes

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