Phosphorylation of acetylhexosamines

Leloir, Luis F.; Cardini, Carlos E.; Olavarría, J.M.

doi:10.1016/0003-9861(58)90201-7

Cited by 45 publications

(8 citation statements)

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“…One was identified as N-acetylglucosamine, the other as N-acetylglucosamine 6-phosphate, the result of the test for hydrolysis-resistant phosphate [Xi], carried out on the latter, being positive. The data of theireaction product identification are summarized in Tables 4 and 5. DISCUSSION N-Acetylglucosamine kinase was described in 1958 by Leloir et al [16], the results of more precise investigations were however published later by Datta in 1970 and 1971 [12,17]. These investigations suggested that the UDP-N-acetylglucosamine and N-acetylglucosamine 6-phosphate are feedback in-…”

Section: Product Of the Reactionmentioning

confidence: 94%

Purification and Properties of N‐Acetylglucosamine Kinase from Human Gastric Mucosa

Gindzieński

Głowacka

Zwiez

1974

European Journal of Biochemistry

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N‐Acetylglucosamine kinase from the human gastric mucous membrane was purified about 170‐fold. The purified enzyme is specific for N‐acetylglucosamine with slight phosphorylation of N‐acetylmannosamine. The aminosugar product of the enzymatic reaction was identified as N‐acetylglucosamine 6‐phosphate. The Km for N‐acetylglucosamine is 0.11 Km and for ATP 3.03 mM. The pded enzyme is stable at +4 °C for three days, labile to dialysis and irreversibly inhibited by p‐chloromercuribenzoate. The molecular weight of the enzyme was 77000.

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Section: Product Of the Reactionmentioning

confidence: 94%

Purification and Properties of N‐Acetylglucosamine Kinase from Human Gastric Mucosa

Gindzieński

Głowacka

Zwiez

1974

European Journal of Biochemistry

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“…Leloir et al (299) have shown that extracts from rat liver and kidney catalyze the ATP-dependent phosphorylation of acetyl glucosamine to the 6-phosphate, and of acetyl galactosamine to the i -phosphate.…”

Section: Pentoses and Related Substancesmentioning

confidence: 99%

Carbohydrate Metabolism

Holzer¹

1959

Annu. Rev. Biochem.

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The following abbreviations are used: A CTH for adrenocorticotropic hormone; ADP for adenosine diphosphate; AMP for adenosine diphosphate; ATP for adenosine triphosphate; DPN for oxidized diphosphopyridine nucleotide; DPNH for reduced diphosphopyridine nucleotide; TPN for oxidized triphosphopyridine nucleotide; TPNH for reduced triphosphopyridine nucleotide; UDP for uridine diphosphate; UMP for uridine monophosphate; UTP for uridine triphosphate. • The author is grateful to Dr. H.-J. Boltze for the translation. 171Annu. Rev. Biochem. 1959.28:171-222. Downloaded from www.annualreviews.org Access provided by University of California -San Francisco UCSF on 02/04/15. For personal use only. Quick links to online content Further ANNUAL REVIEWSIn pancreatic j uice of the rat, the concentration of a-amylase is often so high that the enzyme crystallizes spontaneously (14).Cellulose metabolism has been investigated in a variety of molds and bacteria [(15 to 23); for a summary see (24)]. According to Hash & King (19,20), various �-glucosidases are present in the fungus Myrothecium verrucaria, the specificity of which is dependent on the chain length of the substrate. Cellobiose was not found to be an obligatory precursor of glucose in cellulose breakdown. "Cellulose dextrins" (hexasaccharides, etc.) may be formed from cellobiose by transglucosidation. High-speed-centrifuged par ticles from Acetobacter xylinum were shown by Glaser (21) to contain an enzyme which produces cellulose from UDP-glucose. Similar to glycogen synthesis from UDP-gl�cose a primer is required, such as cellodextrins.In various grasses, structure, synthesis, and breakdown of polyfructosans have been investigated in their dependence upon various, particularly sea sonal conditions by Schlubach (25). Avigad & Feingold (26) investigated the fructosides produced ' from sucrose by a corynebacterium. For the synthesis of hyaluronic acid in streptococci, it has been reported by Markovitz et al. (27) that glucose is a precursor of the glucuronic acid and glucosamine moieties. Tritiated UDP-glucuronic acid together with UDP-N-acetyl glucosamine, ATP, and N-acetyl glucosamine-l-phosphate were incubated with strain A streptococci and found to produce appreciable Annu. Rev. Biochem. 1959.28:171-222. Downloaded from www.annualreviews.org Access provided by University of California -San Francisco UCSF on 02/04/15. For personal use only. CARBOHYDRATE METABOLISM 173 amounts of hyaluronic acid. This indicates that the synthesis of hyaluronic acid is very likely to occur via the UDP compounds. The occurrence in group A streptococci of the UDP compounds mentioned has been ascertained chromatographically (28).Glaser & Brown (29) reported that the formation of chitin in a cell-free preparation from Neurospora crassa utilizes UDP-N-acetyl glucosamine, and requires an acetyl glucosamine polymer as a primer:UDP-acetyl glucosamine + (acetyl glucosamine),,� UDP + (acetyl g!ucosamine)n-t1 (2) The decomposition of chitin has been investigated by Berger & Reynolds (30) with a chiti...

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“…Working on evidence (M. B. Allen, J. L. Brocklebank & D. G. Walker, unpublished observations) that isoenzyme GKa may in fact be N-acetyl-D-glucosamine kinase (EC 2.7.1.59), which possesses some reactivity towards glucose as a substrate, a possibility strengthened by a preliminary report by Davagnino & Ureta (1978), we now report on the isolation of this enzyme from rat liver and kidney tissue, and its characterization. Leloir et al (1958) first reported the presence of N-acetyl-D-glucosamine kinase activity in (NH4)2SO4 fractions prepared from rat liver and kidney. The enzyme has been purified 110-fold from rat liver and shown to have a Km for N-acetyl-D-glucosamine of 0.06 mm and to be inhibited by ADP (Saeki et al, 1971).…”

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confidence: 99%

The isolation and preliminary characterization of N-acetyl-D-glucosamine kinase from rat kidney and liver

Allen¹,

Walker²

1980

Biochemical Journal

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1. Procedures for the extensive purification in high yield of N-acetyl-D-glucosamine kinase from rat liver and kidney are described. The separation of this enzyme from hepatic glucokinase depended primarily on their differing behaviour on an affinity column of Sepharose--N-(6-aminohexanoyl)-2-amino-2-deoxy-D-glucopyranose. 2. This N-acetyl-D-glucosamine kinase also catalyses the phosphorylation of N-acetyl-D-mannosamine and, at a lower rate, several other sugar analogues, including D-glucose. 3. A comparison of the behaviour of the enzyme during gel filtration and electrophoresis in sodium dodecyl sulphate/polyacrylamide gels suggests that N-acetyl-D-glucosamine kinase is a symmetrical dimer of mol.wt. 80000.

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Phosphorylation of acetylhexosamines

Cited by 45 publications

References 16 publications

Purification and Properties of N‐Acetylglucosamine Kinase from Human Gastric Mucosa

Purification and Properties of N‐Acetylglucosamine Kinase from Human Gastric Mucosa

Carbohydrate Metabolism

The isolation and preliminary characterization of N-acetyl-D-glucosamine kinase from rat kidney and liver

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