Disease relevance of adk

• Adenylate kinase, the product of the adk locus in Escherichia coli K12, catalyzes the conversion of AMP and ATP to two molecules of ADP [1].
• The adk gene from Mycobacterium tuberculosis codes for an enzyme of 181 amino acids [2].
• Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+ [3].
• In this work, we identified and characterized the adenylate kinase activity in extracts from the flagellated parasite Trypanosoma cruzi, the causative agent of Chagas' disease [4].

High impact information on adk

• The reported amino acid sequence of mitochondrial adenylate kinase from bovine heart corresponded to AK2A [5].
• Both the products reverted the temperature-sensitive phenotype of the adenylate kinase mutant of E. coli [5].
• Two cDNA clones for mitochondrial adenylate kinase were isolated from a cDNA library of bovine liver poly(A)+ RNA by using synthetic oligodeoxynucleotides as probes [5].
• Adenylate kinase comprises up to 40% of the soluble cellular extracts from E. coli strains containing these plasmids [6].
• The bound Zn2+ atom is demonstrably structural in nature, with no contacts other than its ligating cysteine residues within 5 A. The B. stearothermophilus adenylate kinase lid appears to be a truncated zinc finger domain, lacking the DNA binding finger, which we have termed a zinc knuckle domain [3].

Chemical compound and disease context of adk

• Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop [7].
• The starting structure for the simulation was assembled from the crystal structures of ECAK complexed with the bisubstrate analog diadenosine pentaphosphate (AP(5)A) and of Bacillus stearothermophilus adenylate kinase complexed with AP(5)A, Mg(2+), and 4 coordinated water molecules, and by deleting 1 phosphate group from AP(5)A [8].
• Associative mechanism for phosphoryl transfer: a molecular dynamics simulation of Escherichia coli adenylate kinase complexed with its substrates [8].

Biological context of adk

• In adenylate kinase these mutations cause smallish changes at the active site [7].
• Genes acrA and plsA fall into different cistrons and are arranged in the order proC-acrA-plasA-purE [9].

Anatomical context of adk

• Adenylate kinase activity was detected in different subcellular fractions and the cytosolic isoform was biochemically characterized [4].

Analytical, diagnostic and therapeutic context of adk

• Crystallization and preliminary X-ray analysis of Escherichia coli adenylate kinase [10].
• Amino acids in the phosphate binding loop of adenylate kinase of Escherichia coli were mutated by site-directed mutagenesis [11].
• Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mn2+ Ap5A, and Mg2+ Ap5A have been determined by X-ray crystallography to resolutions of 1.6 A, 1.85 A, and 1.96 A, respectively [3].
• Six different genes of adenylate kinase isoforms were identified and the mRNA expression was confirmed by RT-PCR and Northern Blot [4].

References