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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

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

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.6 Aspergillus fumigatus Q7Z8P9
-
-
2.7.4.6 Aspergillus fumigatus Af293 Q7Z8P9
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.6
-
 Aspergillus fumigatus

Subunits

EC Number Subunits Comment Organism
2.7.4.6 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

EC Number Synonyms Comment Organism
2.7.4.6 AfNDK
-
 Aspergillus fumigatus
2.7.4.6 SwoH
-
 Aspergillus fumigatus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.6 40.6
-
 melting temperature of V83F mutant protein Aspergillus fumigatus
2.7.4.6 57.9
-
 melting temperature of wild-type enzyme Aspergillus fumigatus

General Information

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