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TitleCrystal Structures and Functional Studies Clarify Substrate Selectivity and Catalytic Residues for the Unique Orphan Enzyme N-Acetyl-D-Mannosamine Dehydrogenase.
Journal, issue, pagesBiochem. J., Vol. 462, Page 499-, Year 2014
Publish dateFeb 25, 2014 (structure data deposition date)
AuthorsSola-Carvajal, A. / Gil-Ortiz, F. / Garcia-Carmona, F. / Rubio, V. / Sanchez-Ferrer, A.
External linksBiochem. J. / PubMed:24969681
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-4cr6:
Crystal structure of the N-acetyl-D-mannosamine dehydrogenase without substrates
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-4cr7:
Crystal structure of the N-acetyl-D-mannosamine dehydrogenase with n-acetylmannosamine
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-4cr8:
Crystal structure of the N-acetyl-D-mannosamine dehydrogenase with NAD
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-HOH:
WATER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-BM3:
2-acetamido-2-deoxy-alpha-D-mannopyranose

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

Source
  • flavobacterium sp. 141-8 (bacteria)
KeywordsOXIDOREDUCTASE / N-ACETYL-D-MANNOSAMINE DEHYDROGENASE / SHORT-CHAIN DEHYDROGENASE/REDUCTASE / SUBSTRATE SELECTIVITY

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