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Literature DB >> 322132

Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.

E Subramanian, I D Swan, M Liu, D R Davies, J A Jenkins, I J Tickle, T L Blundell.

Abstract

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.

Entities: Disease Species

Mesh：

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Year: 1977 PMID： 322132 PMCID： PMC392329 DOI： 10.1073/pnas.74.2.556

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

16 in total

1. The low resolution structure analysis of an acid proteinase from Endothia parasitica.

Authors: J A Jenkins; T L Blundell; I J Tickle; L Ungaretti
Journal: J Mol Biol Date: 1975-12-25 Impact factor: 5.469

2. The amino terminal sequences of acid proteases-human pepsin and gastricsin and the protease of Rhizopus chinensis.

Authors: P Sepulveda; K W Jackson; J Tang
Journal: Biochem Biophys Res Commun Date: 1975-04-21 Impact factor: 3.575

3. Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin).

Authors: V B Pedersen; B Foltmann
Journal: Eur J Biochem Date: 1975-06-16

4. The crystal structure of penicillopesin at 6 A resolution.

Authors: I N Hsu; T Hofmann; S C Nyburg
Journal: Biochem Biophys Res Commun Date: 1976-09-07 Impact factor: 3.575

Review 5. The mechanism of the catalytic action of pepsin and related acid proteinases.

Authors: J S Fruton
Journal: Adv Enzymol Relat Areas Mol Biol Date: 1976

6. Biological activity of pepstatins, pepstanone A and partial peptides on pepsin, cathepsin D and renin.

Authors: T Aoyagi; H Morishima; R Nishizawa; S Kunimoto; T Takeuchi
Journal: J Antibiot (Tokyo) Date: 1972-12 Impact factor: 2.649

7. Specific chemical modifications of acid proteases in the presence and absence of pepstatin.

Authors: K Takahashi; W J Chang
Journal: J Biochem Date: 1973-03 Impact factor: 3.387

8. Structure of yeast phosphoglycerate kinase.

Authors: T N Bryant; H C Watson; P L Wendell
Journal: Nature Date: 1974-01-04 Impact factor: 49.962

9. An x-ray crystallographic study of the rennin-like enzyme of Endothia parasitica.

Authors: P C Moews; C W Bunn
Journal: J Mol Biol Date: 1970-12-14 Impact factor: 5.469

10. Effect of pepstatin on acid proteases.

Authors: T Aoyagi; S Kunimoto; H Morishima; T Takeuchi; H Umezawa
Journal: J Antibiot (Tokyo) Date: 1971-10 Impact factor: 2.649

11 in total

1. Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building.

Authors: A A Adzhubei; M J Sternberg
Journal: Protein Sci Date: 1994-12 Impact factor: 6.725

2. Structure of the human renin gene.

Authors: H Miyazaki; A Fukamizu; S Hirose; T Hayashi; H Hori; H Ohkubo; S Nakanishi; K Murakami
Journal: Proc Natl Acad Sci U S A Date: 1984-10 Impact factor: 11.205

Review 3. Fluorescence studies on the active sites of proteinases.

Authors: J S Fruton
Journal: Mol Cell Biochem Date: 1980-09-15 Impact factor: 3.396

Review 4. Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Authors: M J North
Journal: Microbiol Rev Date: 1982-09

5. Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.

Authors: K Suguna; E A Padlan; C W Smith; W D Carlson; D R Davies
Journal: Proc Natl Acad Sci U S A Date: 1987-10 Impact factor: 11.205

6. Comparative X-ray crystallographic evidence for a beta-bend conformation as the active structure for peptide T in T4 receptor recognition.

Authors: J Chen; A Barber; J Pedersen; P W Brandt-Rauf; J Carucci; R B Murphy; R P Carty; D Licht; M R Pincus
Journal: J Protein Chem Date: 1989-02

10. alpha-Bromo-4-amino-3-nitroacetophenone, a new reagent for protein modification. Modification of the methionine-290 residue of porcine pepsin.

Authors: N I Tarasova; G I Lavrenova; V M Stepanov
Journal: Biochem J Date: 1980-05-01 Impact factor: 3.857