Open AccessHomology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Author(s) -
E. Subramanian,
I.D.A. Swan,
Mamie Liu,
David R. Davies,
John A. Jenkins,
Ian J. Tickle,
Tom L. Blundell
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.2.556
Subject(s) - proteases , biochemistry , enzyme , rhizopus , homology (biology) , homology modeling , biology , amino acid , chemistry , stereochemistry , fermentation
The molecular structures of two fungal acid proteases at 3 A resolution have been compared, and found to have similar secondary and tertiary folding. These enzymes are bilobal and have a pronounced cleft between the two lobes. This cleft has been identified as the active site region from inhibitor binding studies. The results of the comparison are discussed in terms of homology among the acid proteases in general.