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Some Clues about Enzymes from Psychrophilic Microorganisms.

Roberta RapuanoGiuseppe Graziano
Published in: Microorganisms (2022)
Enzymes purified from psychrophilic microorganisms prove to be efficient catalysts at low temperatures and possess a great potential for biotechnological applications. The low-temperature catalytic activity has to come from specific structural fluctuations involving the active site region, however, the relationship between protein conformational stability and enzymatic activity is subtle. We provide a survey of the thermodynamic stability of globular proteins and their rationalization grounded in a theoretical approach devised by one of us. Furthermore, we provide a link between marginal conformational stability and protein flexibility grounded in the harmonic approximation of the vibrational degrees of freedom, emphasizing the occurrence of long-wavelength and excited vibrations in all globular proteins. Finally, we offer a close view of three enzymes: chloride-dependent α-amylase, citrate synthase, and β-galactosidase.
Keyphrases
  • molecular dynamics simulations
  • molecular dynamics
  • single molecule
  • protein protein
  • amino acid
  • energy transfer
  • hydrogen peroxide
  • nitric oxide
  • human health
  • metal organic framework
  • quantum dots