Conserved main‐chain peptide distortions: A proposed role for Ile203 in catalysis by dihydrodipicolinate synthase-Reference-Cited by-同舟云学术

Conserved main‐chain peptide distortions: A proposed role for Ile203 in catalysis by dihydrodipicolinate synthase

Published:2008-12 Issue:12 Volume:17 Page:2080-2090
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Dobson Renwick C.J.¹²,Griffin Michael D.W.¹²,Devenish Sean R.A.³,Pearce F. Grant³,Hutton Craig A.²⁴,Gerrard Juliet A.³,Jameson Geoffrey B.⁵,Perugini Matthew A.¹²

Affiliation:

1. Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria 3010, Australia

2. Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia

3. School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand

4. School of Chemistry, University of Melbourne, Parkville, Victoria 3010, Australia

5. Centre for Structural Biology, Institute of Fundamental Sciences, Massey University, Palmerston North 4442, New Zealand

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.037440.108

Reference39 articles.

1. Expression from theEscherichia coli dapApromoter is regulated by intracellular levels of diaminopimelic acid

2. Biochemical evidence that Escherichia coli hyi (orf b0508, gip) gene encodes hydroxypyruvate isomerase

3. Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme

4. Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1.94 Å resolution

5. Reaction Mechanism of Escherichia coli Dihydrodipicolinate Synthase Investigated by X-ray Crystallography and NMR Spectroscopy,

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