PUBLICATION

Dissecting the key residues crucial for the species-specific thermostability of muscle-type creatine kinase

Authors
Gao, Y.S., Wang, Y., Li, C., Chen, Z., Yan, Y.B., and Zhou, H.M.
ID
ZDB-PUB-100621-40
Date
2010
Source
International journal of biological macromolecules   47(3): 366-370 (Journal)
Registered Authors
Wang, Yin
Keywords
muscle-type creatine kinase, species-specific stability, thermostability, body temperature, molecular adaptation
MeSH Terms
  • Adaptation, Physiological
  • Amino Acid Sequence
  • Animals
  • Cattle
  • Conserved Sequence
  • Creatine Kinase, MM Form/chemistry*
  • Creatine Kinase, MM Form/metabolism
  • Dogs
  • Enzyme Stability
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Rabbits
  • Sequence Alignment
  • Species Specificity
  • Temperature*
  • Thermodynamics
  • Zebrafish
PubMed
20558199 Full text @ Int. J. Biol. Macromol.
Abstract
Species-specific protein thermal stability is closely correlated to the living conditions of the organism, especially to its body temperature. In this research, human and zebrafish muscle-type creatine kinases (MMCKs) were taken as model proteins to investigate the molecular adaptation of proteins in poikilothermal and homoiothermal animals. Both the optimal temperature for catalysis and the thermal stability of human MMCK was much higher than those of zebrafish MMCK. Sequence alignment identified 9 amino acid variations conserved in either the teleost MMCKs or the mammal and electric ray MMCKs. Bidirectional mutations were performed to find the residues with beneficial mutations. The results showed that two residues close to the dimer interface of MMCK, the 46(th) and 146(th) residue, were crucial for species-specific thermal stability.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping