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Literature summary for 5.4.99.9 extracted from

  • Mehra-Chaudhary, R.; Dai, Y.; Sobrado, P.; Tanner, J.J.
    In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction (2016), Biochemistry, 55, 833-836 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.99.9

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme mutant H63A with bound UDP-alpha-D-galactopyranose substrate, X-ray diffraction structure determination and analysis. In crystallo capture of a covalent intermediate in the UDP-galactopyranose mutase reaction, structure analysis, detailed overview Aspergillus fumigatus

Protein Variants

Protein Variants Comment Organism
H63A site-directed mutagenesis, inactive mutant Aspergillus fumigatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-galactopyranose Aspergillus fumigatus
-
 UDP-alpha-D-galactofuranose
-
 r

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q4W1X2 i.e. Neosartorya fumigata
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-alpha-D-galactopyranose
-
 Aspergillus fumigatus UDP-alpha-D-galactofuranose
-
 r

Synonyms

Synonyms Comment Organism
UGM
-
 Aspergillus fumigatus

Cofactor

Cofactor Comment Organism Structure
FAD structure analysis reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD Aspergillus fumigatus

General Information

General Information Comment Organism
malfunction the UGM H63A lacks catalytic activity Aspergillus fumigatus
additional information structure analysis reveals UDP bound in the active site and galactopyranose linked to the FAD through a covalent bond between the anomeric C of galactopyranose and N5 of the FAD. The structure confirms the role of the flavin as nucleophile and supports the hypothesis that the proton destined for O5 of galactofuranose is shuttled from N5 of the FAD via O4 of the FAD. His63 is part of the conserved histidine loop, which has the sequence GGHVIF in AfUGM. All UGMs have Gly and His at positions 1 and 3 of the loop, respectively. The conformation of the His loop of AfUGM depends on the redox state of the flavin. The protein-flavin interactions are thought be essential for maintaining the active conformation of UGM Aspergillus fumigatus
physiological function UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in pathogens by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose Aspergillus fumigatus