The Crystal and Solution Studies of Glucosamine-6-phosphate Synthase from Candida albicans

• Published in: Journal of molecular biology Vol. 372; no. 3; pp. 672 - 688
• Main Authors: Raczynska, Joanna, Olchowy, Jaroslaw, Konariev, Peter V., Svergun, Dmitri I., Milewski, Slawomir, Rypniewski, Wojciech
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 21.09.2007
• Subjects: aldose/ketose isomerase; Amino Acid Sequence; Bacterial Proteins - chemistry; Binding Sites; Candida albicans; Candida albicans - enzymology; crystal structure; Crystallography, X-Ray; Escherichia coli; Escherichia coli - enzymology; Fructosephosphates - metabolism; glucosamine-6-phosphate synthase; Glucose-6-Phosphate - metabolism; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing) - chemistry; Isomerases - metabolism; Ligands; Metals - metabolism; Models, Molecular; Molecular Sequence Data; Protein Structure, Quaternary; Protein Structure, Secondary; Scattering, Small Angle; solution structure; Solutions; Static Electricity; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine - metabolism; X-Ray Diffraction; MM; Glc-6-P; aldose/ketose isomerase; GlmS; ISOM; GAH; SAXS; UDP-GlcNAc; ADGP; glucosamine-6-phosphate synthase; Fru-6-P; r.m.s.d; GlcN-6-P; ADMP; crystal structure; solution structure; Gfa1p

Glucosamine 6-phosphate (GlcN-6-P) synthase is an ubiquitous enzyme that catalyses the first committed step in the reaction pathway that leads to formation of uridine 5′-diphospho- N-acetyl-D-glucosamine (UDP-GlcNAc), a precursor of macromolecules that contain amino sugars. Despite sequence similari...