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Literature summary for 2.7.4.3 extracted from

  • Liu, R.; Xu, H.; Wei, Z.; Wang, Y.; Lin, Y.; Gong, W.
    Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion (2009), Biochem. Biophys. Res. Commun., 379, 92-97.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
mutant enzyme L171P, hanging drop vapor diffusion method, 4°C under conditions of 1.22-1.28 M (NH4)2SO4 and 0.1 M Tris-HCl, pH 8.5 Homo sapiens

Protein Variants

Protein Variants Comment Organism
L171P the mutation dramatically changes the orientation of the LID domain, which can be described as a twisted and closed conformation in contrast to the open and closed conformations in other adenylate kinases Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27144
-
-

Purification (Commentary)

Purification (Comment) Organism
Sepharose column chromatography and Superdex 75 gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
Homo sapiens ADP + ADP
-
?

Synonyms

Synonyms Comment Organism
adenylate kinase 4
-
Homo sapiens
AK4
-
Homo sapiens

General Information

General Information Comment Organism
physiological function adenylate kinase 4 is a unique member of the adenylate kinases family which shows no enzymatic activity in vitro Homo sapiens