Abstract
L-Glutamine:d-fructose-6-phosphate amidotransferase, also known as glucosamine-6-phosphate synthase (GlcN6P synthase), which catalyzes the first step in a pathway leading to the formation of uridine 5'-diphospho-N-acetyl-d-glucosamine (UDP-GlcNAc), is a key point in the metabolic control of the biosynthesis of amino sugar-containing macromolecules. The molecular mechanism of the reaction catalyzed by GlcN6P synthase is complex and involves amide bond cleavage followed by ammonia channeling and sugar isomerization. This article provides a comprehensive overview of the present knowledge on this multi-faceted enzyme emphasizing the progress made during the last five years.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Ammonia / metabolism
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Animals
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism
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Candida albicans / enzymology
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Catalysis
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Enzyme Activation
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Gene Expression Regulation, Enzymologic
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Glucose / metabolism
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Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / biosynthesis
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Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / chemistry
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Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) / metabolism*
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Humans
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Isomerism
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Kinetics
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Models, Molecular*
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Structure-Activity Relationship
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Thermodynamics
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Uridine Diphosphate N-Acetylglucosamine / metabolism*
Substances
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Bacterial Proteins
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Fungal Proteins
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Uridine Diphosphate N-Acetylglucosamine
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Ammonia
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Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing)
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Glucose