Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action-Reference-Cited by-同舟云学术

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Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action

Published:2011-12-13 Issue:3 Volume:26 Page:1161-1171
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

Bansal Saurabh¹,Srivastava Ankit²,Mukherjee Goutam³,Pandey Ramendra⁴,Verma Anita Kamra⁴,Mishra Prashant¹,Kundu Bishwajit¹

Affiliation:

1. Department of Biochemical Engineering and BiotechnologyIndian Institute of Technology DelhiNew DelhiIndia

2. Kusuma School of Biological SciencesIndian Institute of Technology DelhiNew DelhiIndia

3. Supercomputing Facility for Bioinformatics and Computational BiologyIndian Institute of Technology DelhiNew DelhiIndia

4. Department of ZoologyKirorimal CollegeDelhi UniversityNew DelhiIndia

Funder

Indian Institute of Technology Delhi

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.11-191254

Reference64 articles.

1. Stability of biocatalysts

2. Enhancing the thermostability of Escherichia coli l-asparaginase II by substitution with pro in predicted hydrogen-bonded turn structures

3. Engineering thermal stability of l-asparaginase by in vitro directed evolution

4. Pegaspargase: a review of clinical studies

5. L-Asparaginase encapsulated intact erythrocytes for treatment of acute lymphoblastic leukemia (ALL)

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