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Literature summary for 2.7.4.6 extracted from

  • Hu, Y.; Jia, X.; Lu, Z.; Han, L.
    Characterization of crystal structure and key residues of Aspergillus fumigatus nucleoside diphosphate kinase (2019), Biochem. Biophys. Res. Commun., 511, 148-153 .
    View publication on PubMed
Search for more literature for 2.7.4.6

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Aspergillus fumigatus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method Aspergillus fumigatus

Protein Variants

Protein Variants Comment Organism
H117Q then active site mutant H117Q loses kinase activity Aspergillus fumigatus
V83F the structure of the mutant enzyme is not stable at higher temperature Aspergillus fumigatus

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus Q7Z8P9
-
-
Aspergillus fumigatus Af293 Q7Z8P9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Aspergillus fumigatus

Subunits

Subunits Comment Organism
tetramer the enzyme exists predominantly in form of tetramer in solution. The tetrameric form with dimer-dimer interaction is crucial for its function. The dimeric enzyme form loses the kinase activity and is lethal for Aspergillus fumigatus Aspergillus fumigatus

Synonyms

Synonyms Comment Organism
AfNDK
-
 Aspergillus fumigatus
SwoH
-
 Aspergillus fumigatus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40.6
-
 melting temperature of V83F mutant protein Aspergillus fumigatus
57.9
-
 melting temperature of wild-type enzyme Aspergillus fumigatus

General Information

General Information Comment Organism
physiological function the enzyme is essential for its viability Aspergillus fumigatus