Total for the last 12 months
number of access : ?
number of downloads : ?
ID 110768
Author
Noma, Takafumi Department of Molecular Biology, Institute of Health Biosciences, The University of Tokushima Graduate School Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
adenine nucleotide
adenylate kinase
high-energy phosphoryl transfer
homeostasis
isozyme
Content Type
Journal Article
Description
Adenylate kinase (hereinafter referred to as AK) catalyzes a reversible high-energy phosphoryl transfer reaction between adenine nucleotides. The enzyme contributes to the homeostasis of cellular adenine nucleotide composition in addition to the nucleotide biosynthesis. So far, six AK isozymes, AK1, AK2, AK3, AK4, AK5, andAK6, were identified.AK1 is localized in neuronal processes, sperm tail and on the cytoskeleton in cardiac cells at high concentrations, suggesting its regulatory function as a high-energyβ-phosphoryl transfer chain from ATP-synthesizing sites to the ATP-utilizing sites in the cell. AK2, AK3 and AK4 are mitochondrial proteins. AK2 is expressed in the intermembrane space, while AK3 and AK4 are localized in the mitochondrial matrix. AK3 is expressed in all tissues except for red blood cells indicating thatAK3 gene is a housekeeping-type gene. On the other hand, AK4is tissue specifically expressed mainly in kidney, brain, heart, and liver although its enzymatic activity is not yet detected. AK5 is solely expressed in a limited area of brain. AK6 is recently identified in nucleus, suggesting its role in nuclear nucleotide metabolism. All data, so far reported, indicated the function of AK is associated with the mechanism of efficient transfer of high-energy phosphate in micro-compartment within the cell.
Journal Title
The journal of medical investigation : JMI
ISSN
13431420
NCID
AA11166929
Volume
52
Issue
3-4
Start Page
127
End Page
136
Sort Key
127
Published Date
2005-08
EDB ID
DOI (Published Version)
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Publisher
departments
Oral Sciences