Isothermal Titration Microcalorimetry Reveals the Cooperative and Noncompetitive Nature of Inhibition of Sinorhizobium meliloti L5-30 Dihydrodipicolinate Synthase by (S)-Lysine-Reference-Cited by-同舟云学术

Isothermal Titration Microcalorimetry Reveals the Cooperative and Noncompetitive Nature of Inhibition of Sinorhizobium meliloti L5-30 Dihydrodipicolinate Synthase by (S)-Lysine

Published:2008-07-01 Issue:30 Volume:47 Page:7779-7781
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Phenix Christopher P.¹,Palmer David R. J.¹

Affiliation:

1. Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Saskatchewan, Canada S7N 5C9

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800629n

Reference22 articles.

1. Structural, Functional and Calorimetric Investigation of MosA, a Dihydrodipicolinate Synthase fromSinorhizobium melilotiL5–30, does not Support Involvement in Rhizopine Biosynthesis

2. Dihydrodipicolinate synthase (DHDPS) from Escherichia coli displays partial mixed inhibition with respect to its first substrate, pyruvate

3. Inhibition of lysine biosynthesis: an evolving antibiotic strategy

4. Inhibiting dihydrodipicolinate synthase across species: Towards specificity for pathogens?

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5. Tyrosine 110 Plays a Critical Role in Regulating the Allosteric Inhibition of Campylobacter jejuni Dihydrodipicolinate Synthase by Lysine;Biochemistry;2014-11-18