Structure of adenylate kinase 1 in complex with P1,P4-di(adenosine) tetraphosphateStructure of adenylate kinase 1 in complex with P1,P4-di(adenosine) tetraphosphate
Structural highlights
2c95 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
KAD1_HUMAN Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:612631.[1][2][3]
Function
KAD1_HUMAN Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A. Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. PMID:2542324
↑Qualtieri A, Pedace V, Bisconte MG, Bria M, Gulino B, Andreoli V, Brancati C. Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia. Br J Haematol. 1997 Dec;99(4):770-6. PMID:9432020
↑Corrons JL, Garcia E, Tusell JJ, Varughese KI, West C, Beutler E. Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia. Blood. 2003 Jul 1;102(1):353-6. Epub 2003 Mar 20. PMID:12649162 doi:10.1182/blood-2002-07-2288
