Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: Comparison with the bacterial collagenase from Achromobacter iophagus
The specificity of the collagenolytic enzyme from the fungus Entomophthora coronata toward some inhibitors and the B chain of oxidized insulin was investigated and compared to that of the bacterial collagenase from Achromobacter iophagus. The fungal enzyme was completely inhibited by diisopropylfluo...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1979-02, Vol.192 (2), p.438-445 |
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Sprache: | eng |
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Zusammenfassung: | The specificity of the collagenolytic enzyme from the fungus
Entomophthora coronata toward some inhibitors and the B chain of oxidized insulin was investigated and compared to that of the bacterial collagenase from
Achromobacter iophagus. The fungal enzyme was completely inhibited by diisopropylfluorophosphate, tosyl-
l-lysine chloromethyl ketone, and tosyl-amino-2-phenylethyl chloromethyl ketone but not at all by ethylenediaminetetraacetate. This indicates that it is not a metalloenzyme like the bacterial
Achromobacter collagenase. The B chain of insulin was not hydrolysed at all by the bacterial enzyme under conditions where extensive digestion was observed with the
Entomophthora enzyme. The fungal enzyme cleaves preferentially the bonds
Leu
15
-
Tyr
16
and
Leu
11
Val
12
as determined by automatic sequencing; the secondary cleavages were identified by a systematic analysis of the digestion mixture; thus, the fungal collagenolytic enzyme from
Entomophthora coronata differs both structurally and functionally from the bacterial
Achromobacter collagenase. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(79)90113-9 |