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Literature summary for 2.7.4.8 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
Search for more literature for 2.7.4.8

Cloned(Commentary)

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

Organic Solvent Stability

Organic Solvent Comment Organism
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
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

Organism UniProt Comment Textmining
Brugia malayi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Brugia malayi

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
BmGK
-
 Brugia malayi

Temperature Stability [°C]

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

General Information

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