Recombinant crab collagenase

Details Recombinant crab collagenase Recombinant crab collagenase

1996-05-09

1998-05-05

Prouty, Rebecca E.

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Hydrolase

435212, 435219, 530857, C12N 964, C12N 948, C12N 950

Patent

active

057473226

ABSTRACT:
An isolated sequence is provided that encodes crab procollagenase (Seq ID NO 5) that upon cleaving off the 29 amino acid propeptide (Seq ID NO 6) transforms into an active collagenase (Seq ID NO 4). The procollagenase has the MW of about 26.6 kD and the mature collagenase has a MW of 23.5 kD. Procollagenase mutated at positions 201 and 235 is also provided. A storage-stabilized composition providing long-term, shelf-stable protease that can be readily activated when collagenolytic activity is desired is disclosed.

REFERENCES:
patent: 5143837 (1992-09-01), Sova et al.
patent: 5418157 (1995-05-01), Lin et al.
Corey et al., "Trypsin Specificity Increased Through Substrate-Assisted Catalysis," Biochemistry, 34, pp. 11521-11527 (1995).
Grant et al., "Amino Acid Sequence of a Collagenolytic Protease Hepatopancreas from the Fiddler Crab, Uca pugilator," Biochemistry, 19, pp. 4653-4659 (1980).
Tsu et al., "The Substrate Specificity of Uca pugilator Collagenolytic Serine Protease 1 Correlates with the Bovine Type I Collagen cleavage Sites," J. Biol. Chem., 269:30, pp. 19565-19572 (1994).
Willett et al., "Engineered Metal Regulation of Trypsin Specificity," Biochemistry, 34, pp. 2172-2180 (1995).
Eisen et al. (1973) Biochemistry 12, 1814-1822.

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