Abstract |
Nucleoside (NDP) diphosphate kinases are oligomeric enzymes. Most are hexameric, but some bacterial enzymes are tetrameric. Hexamers and tetramers are constructed by assembling identical dimers. The hexameric structure is important for protein stability, as demonstrated by studies with natural mutants (the Killer-of-prune mutant of Drosophila NDP kinase and the S120G mutant of the human NDP kinase A in neuroblastomas) and with mutants obtained by site-directed mutagenesis. It is also essential for enzymic activity. The function of the tetrameric structure is unclear.
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Authors | L Lascu, A Giartosio, S Ransac, M Erent |
Journal | Journal of bioenergetics and biomembranes
(J Bioenerg Biomembr)
Vol. 32
Issue 3
Pg. 227-36
(Jun 2000)
ISSN: 0145-479X [Print] United States |
PMID | 11768306
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Nucleoside-Diphosphate Kinase
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Topics |
- Amino Acid Sequence
- Animals
- Crystallography, X-Ray
- Evolution, Molecular
- Humans
- Molecular Sequence Data
- Mutagenesis
- Nucleoside-Diphosphate Kinase
(chemistry, genetics)
- Protein Structure, Quaternary
- Sequence Homology, Amino Acid
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