Literature summary for 3.4.24.25 extracted from

Adekoya, O.A.; Helland, R.; Willassen, N.P.; Sylte, I.
Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family (2006), Proteins, 62, 435-449.

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Organism

Organism	UniProt	Comment	Textmining
Antarctic bacterium str. 643	Q9KH34	precursor	-

Subunits

Subunits	Comment	Organism
More	comparative sequence-structure analysis and molecular dynamics simulations to reveal the molecula features of cold adaptation of enzyme. Enzyme has fewer arginines, a lower Arg/(Lys+Arg) ratio, a lower fraction of large aliphatic residues, more methionines, more serines, and more of the thermolabile amino acid asparagine than other thermolysin enzymes. Additionally, the enzyme has fewer intramolecular cation-pi electron interactions and fewer hydrogen bonds than its pseudolysin or thermolysin counterparts	Antarctic bacterium str. 643

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Release 2023.1 (January 2023)