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Chemical and enzymatic properties of four collagenases newly isolated from anaerobic Clostridium histolyticum, aerobic Achromobacter iophagus, and from two lower eucaryotes, the fungus Entomophthora coronata and the insect Hypoderma lineatum are reviewed. The problems of their biosynthesis and precursors, namely the effect of induction of collagenase and neutral proteinase in Achromobacter by their macromolecular substrates are discussed. The two bacterial collagenases are Zn-metallo-enzymes; the highly purified Clostridium collagenase contains cyst(e)ine, serine phosphate and tryptophan additionally to amino acids reported previously. Achromobacter collagenase has the highest specific activity of all collagenases; it yields by autolysis enzymatically active degraded forms. The active dimer is composed of two identical subunits of molecular weight 35,000. Similarities between Achromobacter collagenase, thermolysin and Bacillus subtilis neutral proteinase in molecular weight, amino acid composition, and amino acids important for the active sites are discussed. The two collagenases from low eucaryotes are serine proteinases; Hypoderma collagenase is homologous to the trypsin family in the amino terminal sequence. The initial cleavage of native collagen by highly purified bacterial collagenases occurs in the central helical part of the alpha chains and not progressively from the amino terminal end. One of the two initial cleavages produced by Achromobacter collagenase is situated in the region cleaved specifically by vertebrate collagenases, but with different bond specificity. The same is true for the insect collagenase. Entomophthora collagenase is a proteinase of broad specificity which also cleaves collagen in its helical parts. All four collagenases also degrade other proteins according to their bond specificity.
Mol Cell Biochem 1979 Jan 26
PMID:Some newly characterized collagenases from procaryotes and lower eucaryotes. 22 May 20

With the determination of the three-dimensional structure of elastase and the probable identification of the active site and key residues involved in proteolytic activity, our knowledge of the molecular details of this interesting protease is rapidly increasing. Pseudomonas elastase appears to be remarkably similar to the Bacillus metalloproteinase thermolysin. A further significant development has been the discovery of the lasA gene and the fact that Pseudomonas elastase and alkaline proteinase appear to act in concert with the LasA protein to display the notable elastolytic activity exhibited by isolates of this organism. Biochemical and genetic studies indicate that LasA is a second elastase which may be an important virulence factor that has been overlooked in previous studies.
Mol Microbiol 1991 Oct
PMID:Pseudomonas aeruginosa elastase and elastolysis revisited: recent developments. 179 48

In the past, the method of reconstitution was used to investigate the interaction between metalloenzymes (containing Zn(II)) and metal ions. In this paper, electron paramagnetic resonance (EPR) has been employed to firstly study the direct interactions between Bacillus subtilis neutral proteinase (BSNP), nuclease P1 and Cu(II) ions added in aqueous solution, respectively. These results show that a dynamic equilibrium exists between the Zn(II) in the active site of native enzymes and the added Cu(II), the added Cu(II) partly replaces the Zn(II), forming Cu(II)-enzyme derivatives. As a result, the activity of the native enzymes is influenced. The influences of pH value on this kind of interaction have also been investigated, and the results demonstrate that the change of pH value has little influence on the system of nuclease P1, but has remarkable influence on BSNP. We firstly obtained the EPR spectra for Cu(II)-enzyme derivatives. In addition, the derivative of Cu(II)-BSNP exists in the solution with two different conformations (I type g(parallel)=2.34, A(parallel) (mT)=13.4; II type g(parallel)=2.25, A(parallel) (mT)=16.1), and this two conformations exchanged each other depending on pH.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Jun
PMID:Applications of electron paramagnetic resonance spectroscopy to study interactions of metalloenzymes with Cu(II) ions. 1273 61