An Expedient Synthesis of Allylic Polyprenyl Phosphates

Branch, Clive L.; Burton, George; Moss, Stephen F.

doi:10.1080/00397919908086425

Cited by 19 publications

(16 citation statements)

References 10 publications

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“…49 The dolichol mixture (0.003 mmol) was dissolved in dry THF (1 mL) under argon, followed by addition of 1- H tetrazole (0.006 g, 0.008 mmol) and diisopropylamino-di-(2-cyanoethoxy)-phosphine (0.03 g, 0.009 mmol). The solution was stirred for 2 h, then cooled to −30 °C, after which 30% hydrogen peroxide (0.2 mL) was added dropwise and the mixture was warmed to room temperature.…”

Section: Methodsmentioning

confidence: 99%

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

et al. 2013

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Asparagine-linked glycosylation is a complex protein modification conserved among all three domains of life. Herein we report the in vitro analysis of N-linked glycosylation from the methanogenic archaeon Methanococcus voltae. Using a suite of synthetic and semisynthetic substrates, we show that AglK initiates N-linked glycosylation in M. voltae through the formation of α-linked dolichyl monophosphate N-acetylglucosamine (Dol-P-GlcNAc), which contrasts with the polyprenyl-diphosphate intermediates that feature in both eukaryotes and bacteria. Intriguingly, AglK exhibits high sequence homology to dolichyl-phosphate β-glucosyltransferases, including Alg5 in eukaryotes, suggesting a common evolutionary origin. The combined action of the first two enzymes, AglK and AglC, afforded an α-linked Dol-P-glycan that serves as a competent substrate for the archaeal oligosaccharyl transferase AglB. These studies provide the first biochemical evidence revealing that despite the apparent similarity of the overall pathways, there are actually two general strategies to achieve N-linked glycoproteins across the domains of life.

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Section: Methodsmentioning

confidence: 99%

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

et al. 2013

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“…For example, Und-P and Dol-P have been chemically synthesized using various approaches. 8,[11][12][13][14][15] However, in general chemical methods are not ideal, because the starting isoprenols are expensive and often only available in very limited quantities (µg-mg) and chemical phosphorylation may be impractical on small scales. In addition, it is difficult to quantify the small amounts of polyprenyl phosphates produced in these reactions.…”

Section: Introductionmentioning

confidence: 99%

Chemoenzymatic synthesis of polyprenyl phosphates

Hartley¹,

Larkin²,

Imperiali³

2008

Bioorganic & Medicinal Chemistry

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Polyprenyl phosphates, including undecaprenyl phosphate and dolichyl phosphate, are essential intermediates in several important biochemical pathways including N-linked protein glycosylation in eukaryotes and prokaryotes and prokaryotic cell wall biosynthesis. Herein, we describe the evaluation of three potential undecaprenol kinases as agents for the chemoenzymatic synthesis of polyprenyl phosphates. Target enzymes were expressed in crude cell envelope fractions and quantified via the use of luminescent lanthanide-binding tags (LBTs). The Streptococcus mutans diacylglycerol kinase (DGK) was shown to be a very useful agent for polyprenol phosphorylation using ATP as the phosphoryl transfer agent. In addition, the S. mutans DGK can be coupled with two Campylobacter jejuni glycosyltransferases involved in N-linked glycosylation to efficiently biosynthesize the undecaprenyl pyrophosphate-linked disaccharide needed for studies of PglB, the C. jejuni oligosaccharyl transferase.

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“…The title compound 2 was synthesized from undecaprenol 1 (52 mg, 0.068 mmol) according to known method: 22 …”

Section: Disodium Undecaprenyl Phosphate (2)mentioning

confidence: 99%

Synthesis of undecaprenyl pyrophosphate-linked glycans as donor substrates for bacterial protein N-glycosylation

2009

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An Expedient Synthesis of Allylic Polyprenyl Phosphates

Cited by 19 publications

References 10 publications

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis

Chemoenzymatic synthesis of polyprenyl phosphates

Synthesis of undecaprenyl pyrophosphate-linked glycans as donor substrates for bacterial protein N-glycosylation

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