Tags

Type your tag names separated by a space and hit enter

Structural characterization of a highly stable cysteine protease ervatamin C.
Biochem Biophys Res Commun. 1999 Nov 02; 264(3):635-42.BB

Abstract

Ervatamin C, a novel cysteine protease, belongs to alpha + beta class of proteins, probably with two domains, and retains both secondary and tertiary structures along with biological activity over a wide range of pH (2-12). Under neutral conditions, GuHCl and temperature-induced unfolding was cooperative with high transition midpoints and shows no structural changes in the presence of urea reflecting a remarkable stability. The fluorescence emission maximum at 350 nm suffers a blue shift of 4-5 nm upon lowering the pH and a red shift of 5 nm under denatured conditions. Unfolding transition curves at pH 2.0 are non-coincidental indicating the presence of intermediates in the unfolding pathway. At extremely low pH, the enzyme loses all the tertiary structure and proteolytic activity but retains a predominant secondary structure and a strong binding to ANS. GuHCl-induced unfolding of the enzyme in this intermediate state is noncooperative and indicates sequential unfolding of the domains.

Authors+Show Affiliations

Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, Varanasi, 221 005, India.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10543984

Citation

Kundu, S, et al. "Structural Characterization of a Highly Stable Cysteine Protease Ervatamin C." Biochemical and Biophysical Research Communications, vol. 264, no. 3, 1999, pp. 635-42.
Kundu S, Sundd M, Jagannadham MV. Structural characterization of a highly stable cysteine protease ervatamin C. Biochem Biophys Res Commun. 1999;264(3):635-42.
Kundu, S., Sundd, M., & Jagannadham, M. V. (1999). Structural characterization of a highly stable cysteine protease ervatamin C. Biochemical and Biophysical Research Communications, 264(3), 635-42.
Kundu S, Sundd M, Jagannadham MV. Structural Characterization of a Highly Stable Cysteine Protease Ervatamin C. Biochem Biophys Res Commun. 1999 Nov 2;264(3):635-42. PubMed PMID: 10543984.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural characterization of a highly stable cysteine protease ervatamin C. AU - Kundu,S, AU - Sundd,M, AU - Jagannadham,M V, PY - 1999/11/2/pubmed PY - 1999/11/2/medline PY - 1999/11/2/entrez SP - 635 EP - 42 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 264 IS - 3 N2 - Ervatamin C, a novel cysteine protease, belongs to alpha + beta class of proteins, probably with two domains, and retains both secondary and tertiary structures along with biological activity over a wide range of pH (2-12). Under neutral conditions, GuHCl and temperature-induced unfolding was cooperative with high transition midpoints and shows no structural changes in the presence of urea reflecting a remarkable stability. The fluorescence emission maximum at 350 nm suffers a blue shift of 4-5 nm upon lowering the pH and a red shift of 5 nm under denatured conditions. Unfolding transition curves at pH 2.0 are non-coincidental indicating the presence of intermediates in the unfolding pathway. At extremely low pH, the enzyme loses all the tertiary structure and proteolytic activity but retains a predominant secondary structure and a strong binding to ANS. GuHCl-induced unfolding of the enzyme in this intermediate state is noncooperative and indicates sequential unfolding of the domains. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/10543984/Structural_characterization_of_a_highly_stable_cysteine_protease_ervatamin_C_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(99)91550-4 DB - PRIME DP - Unbound Medicine ER -