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Literature summary extracted from

  • Gupta, S.; Yadav, S.; Suryanarayanan, V.; Singh, S.K.; Saxena, J.K.
    Investigating the folding pathway and substrate induced conformational changes in B. malayi Guanylate kinase (2017), Int. J. Biol. Macromol., 94, 621-633 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.8 expression in Escherichia coli BL21 (DE3) Brugia malayi

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
2.7.4.8 guanidine-HCl guanidine-HCl unfolding shows monomer molten globule like intermediate at 0.8-1.0 M. Protective role of substrates in maintaining the integrity of the enzyme Brugia malayi
2.7.4.8 urea 1-2 M, an inactive, partially unfolded, dimeric intermediate is observed. Protective role of substrates in maintaining the integrity of the enzyme Brugia malayi

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.8 Brugia malayi
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.8
-
 Brugia malayi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.8 ATP + GMP
-
 Brugia malayi ADP + GDP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.8 BmGK
-
 Brugia malayi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.4.8 additional information
-
 thermostability of the enzyme is found to be significantly enhanced in the presence of the substrates Brugia malayi

General Information

EC Number General Information Comment Organism
2.7.4.8 metabolism guanylate kinase is one of the key enzymes in nucleotide biosynthesis Brugia malayi