Semisynthetic enzymes: apoproteins from heme proteins as hydrola

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing oxygen-containing organic compound

Patent

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

435140, 435141, 435155, 435160, 435161, 435197, 530385, 530402, C12P 702, C12P 706, C12P 716, C12P 740, C12P 754, C12P 752, C12N 918, C07K 1300

Patent

active

047644648

ABSTRACT:
Proteins having a hydrophobic cavity proximate to which is a residue promoting hydrolysis of functional moieties are effective semisynthetic hydrolases. Heme proteins from which the heme has been removed usually have at least one imidazole residue proximate to the cavity, and thus act as quite effective esterases. Because the size and shape of the cavities of such proteins are capable of broad diversity a wide spectrum of substrates may be hydrolyzed by these semisynthetic enzymes.

REFERENCES:
Gratecos, D. and Fischer, E. H., (1974) Biochem. Biophys. Res. Commun. 58, 960-967.
R. Breslow, Science, 218, 532 (1982).
Cram, J. Am. Chem. Soc., 105, 135 (1983).
Breslow, J. Am. Chem. Soc., 103, 154 (1981).
Klotz, Proc. Natl. Acad. Sci., 68 (2), 263 (1971).

LandOfFree

Say what you really think

Search LandOfFree.com for the USA inventors and patents. Rate them and share your experience with other people.

Rating

Semisynthetic enzymes: apoproteins from heme proteins as hydrola does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Semisynthetic enzymes: apoproteins from heme proteins as hydrola, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Semisynthetic enzymes: apoproteins from heme proteins as hydrola will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFUS-PAI-O-600380

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.