[Collagenolytic enzymes synthesized by microorganisms].
The review uses data obtained by the authors and available in the literature to discuss microbial collagenolytic enzymes, widely employed in scientific research, biotechnology, and medicine. Collagenases differing in their structure and the specificity of their action on collagen fibrils were isolated from bacteria (including marine isolates), actinomycetes, and fungi. Collagenases produced by Clostridium histolyticum and Achromobacter iophagus are the best studied enzymes; both are metalloenzymes that contain Zn2+ in their active site and retain collagenolytic activity in the presence of Ca2+. Serine-type collagenolytic proteases were also found in microorganisms. These enzymes differ from "true" collagenases by the structure of their active site. Both serine proteases and metalloproteases with high collagenolytic activities were isolated from the culture liquids of Streptomyces and Actinomyces strains. The biosynthesis of collagenases is induced by the addition of various collagen-containing substrates to the cultivation medium.
Demina
N S
NS
Lysenko
S V
SV
D000190:Actinomyces / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology*; D003013:Clostridium / Q000201:enzymology; D003094:Collagen / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D017364:Collagenases / Q000096:biosynthesis*; D010450:Endopeptidases / Q000096:biosynthesis*; D012697:Serine Endopeptidases / Q000096:biosynthesis; D013329:Structure-Activity Relationship
D003094:Collagen; D010450:Endopeptidases; D012697:Serine Endopeptidases; D017364:Collagenases