The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase

Conserva, Francesca; Panayiotou, Christakis; Karlsson, Anna; Solaroli, Nicola

doi:10.1016/j.biocel.2013.02.004

Cited by 44 publications

(29 citation statements)

References 17 publications

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“…In addition, a recent study using GFP-fusion proteins demonstrated AK9 in both cytosolic and nuclear compartments [13]. Cytosolic and organellar AK isozymes maintain adenine nucleotide homeostasis via the reaction; Mg 2+ -ATP (or GTP) + AMP ↔ Mg 2+ -ADP (or GDP) + ADP.…”

Section: Introductionmentioning

confidence: 99%

Differential Expression of Adenine Nucleotide Converting Enzymes in Mitochondrial Intermembrane Space: A Potential Role of Adenylate Kinase Isozyme 2 in Neutrophil Differentiation

et al. 2014

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Adenine nucleotide dynamics in the mitochondrial intermembrane space (IMS) play a key role in oxidative phosphorylation. In a previous study, Drosophila adenylate kinase isozyme 2 (Dak2) knockout was reported to cause developmental lethality at the larval stage in Drosophila melanogaster. In addition, two other studies reported that AK2 is a responsible gene for reticular dysgenesis (RD), a human disease that is characterized by severe combined immunodeficiency and deafness. Therefore, mitochondrial AK2 may play an important role in hematopoietic differentiation and ontogenesis. Three additional adenine nucleotide metabolizing enzymes, including mitochondrial creatine kinases (CKMT1 and CKMT2) and nucleoside diphosphate kinase isoform D (NDPK-D), have been found in IMS. Although these kinases generate ADP for ATP synthesis, their involvement in RD remains unclear and still an open question. In this study, mRNA and protein expressions of these mitochondrial kinases were firstly examined in mouse ES cells, day 8 embryos, and 7-week-old adult mice. It was found that their expressions are spatiotemporally regulated, and Ak2 is exclusively expressed in bone marrow, which is a major hematopoietic tissue in adults. In subsequent experiments, we identified increased expression of both AK2 and CKMT1 during macrophage differentiation and exclusive production of AK2 during neutrophil differentiation using HL-60 cells as an in vitro model of hematopoietic differentiation. Furthermore, AK2 knockdown specifically inhibited neutrophil differentiation without affecting macrophage differentiation. These data suggest that AK2 is indispensable for neutrophil differentiation and indicate a possible causative link between AK2 deficiency and neutropenia in RD.

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Section: Introductionmentioning

confidence: 99%

Differential Expression of Adenine Nucleotide Converting Enzymes in Mitochondrial Intermembrane Space: A Potential Role of Adenylate Kinase Isozyme 2 in Neutrophil Differentiation

et al. 2014

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“…AK9 is a nucleoside mono-and diphosphate kinase due to its broad phosphatase activity, the local concentration of substrates probably influences catalytic activity [21,30]. The AK9 gene is located on the chromosome 6 on the location 6q21 (NCBI Gene ID: 221264).…”

Section: Adenylate Kinases Found In Nucleusmentioning

confidence: 99%

Adenylate Kinase: A Ubiquitous Enzyme Correlated with Medical Conditions

Ionescu

2019

Protein J

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Adenylate kinase is a small, usually monomeric, enzyme found in every living thing due to its crucial role in energetic metabolism. This paper outlines the most relevant data about adenylate kinases isoforms, and the connection between dysregulation or mutation of human adenylate kinase and medical conditions. The following datadases were consulted: National Centre for Biotechnology Information, Protein Data Bank, and Mouse Genomic Informatics. The SmartBLAST tool, EMBOSS Needle Program, and Clustal Omega Program were used to analyze the best protein match, and to perform pairwise sequence alignment and multiple sequence alignment. Human adenylate kinase genes are located on different chromosomes, six of them being on the chromosomes 1 and 9. The adenylate kinases' intracellular localization and organ distribution explain their dysregulation in many diseases. The cytosolic isoenzyme 1 and the mitochondrial isoenzyme 2 are the main adenylate kinases that are integrated in the vast network of inflammatory modulators. The cytosolic isoenzyme 5 is correlated with limbic encephalitis and Leu673Pro mutation of the isoenzyme 7 leads to primary male infertility due to impairment of the ciliary function. The impairment of the mitochondrial isoenzymes 2 and 4 is demonstrated in neuroblastoma or glioma. The adenylate kinases are disease modifier that can assess the risk of diseases where oxidative stress plays a crucial role in pathogenesis like metabolic syndrome or neurodegenerative diseases. Because adenylate kinases has ATP as substrate, they are integrated in the global network of energetic process of any organism therefore are valid target for new pharmaceutical compounds. Keywords Adenylate kinase • Nucleotide metabolism • Phosphotransfer enzymes • AMP-activated protein kinase • Adenine nucleotide • Homeostasis Abbreviations ADP Adenosine diphosphate AK Adenylate kinase AMP Adenosine monophosphate AMPK AMP-activated protein kinases Ap5A P1,P5-di(adenosine-5′) pentaphosphate ATP Adenosine triphosphate B4P Bis(adenosine)-5′-tetraphosphate BLAST Basic local alignment search tool BLOSUM BLOcks SUbstitution Matrix CDP Cytidine diphosphate dNTP Deoxy-nucleoside triphosphates DGYP Aspartic acid glycine tyrosine proline GTP

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“…As the phosphotransferase, several isoforms of Adenylate kinase existed in mammalian tissues was well documented (Dzeja & Terzic, 2009). Marjan Amiri reported that AKI catalysed the phosphorylation of AMP and CMP with GTP as phosphate donor, while AMP, dAMP, CMP and dCMP were all phosphorylated when ATP was the phosphate donor (Amiri et al, 2013). Three phosphorylation sites, including S38, S178 and S181, have been identified in adenylate kinase in human skeletal muscle (Højlund et al, 2009).…”

Section: Relationship Between Protein Phosphorylation and Glycolytic mentioning

confidence: 99%

The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

Chen

et al. 2018

Int J of Food Sci Tech

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Protein phosphorylation is a key modulator in glycolysis metabolism and regulates the activity of glycometabolic enzymes. The phosphorylation levels of sarcoplasmic proteins were investigated in relationship to the glycolysis rate in postmortem ovine muscle in the present study. The global phosphorylation levels of sarcoplasmic proteins increased early postmortem and then decreased afterwards in postmortem ovine muscle. Protein bands of different phosphorylation levels were identified as glycometabolism‐related enzymes. The phosphorylation levels of Glycogen phosphorylase and Pyruvate kinase maybe one possible reason for the different glycolytic rates at 0.5 h postmortem. The glycolytic rate attributes were negatively correlated with four bands which were probably phosphofructokinase, enolase and adenylate kinase isoenzyme. In summary, the phosphorylation of sarcoplasmic proteins is related to muscle pH decline early postmortem, influencing the meat rigour mortis and quality development.

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The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase

Cited by 44 publications

References 17 publications

Differential Expression of Adenine Nucleotide Converting Enzymes in Mitochondrial Intermembrane Space: A Potential Role of Adenylate Kinase Isozyme 2 in Neutrophil Differentiation

Differential Expression of Adenine Nucleotide Converting Enzymes in Mitochondrial Intermembrane Space: A Potential Role of Adenylate Kinase Isozyme 2 in Neutrophil Differentiation

Adenylate Kinase: A Ubiquitous Enzyme Correlated with Medical Conditions

The effect of sarcoplasmic protein phosphorylation on glycolysis in postmortem ovine muscle

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