1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/article/10.1007/s12104-017-9747-6/fulltext.html
Reference24 articles.
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2. Britton J, Meneghini LM, Raston CL, Weiss GA (2016) Accelerating enzymatic catalysis using vortex fluidics. Angew Chem Int Edit 55:11387–11391. doi: 10.1002/anie.201604014
3. Cao T-P, Kim J-S, Woo M-H, Choi JM, Jun Y, Lee KH, Lee SH (2016) Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis. J Microbiol 54:311–321. doi: 10.1007/s12275-016-6029-4
4. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
5. Dick M et al (2016a) Mechanism-based inhibition of an aldolase at high concentrations of its natural substrate acetaldehyde: structural insights and protective strategies. Chem Sci 7:4492–4502
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact;Applied Microbiology and Biotechnology;2021-08
2. Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis;ACS Catalysis;2018-03-27
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