In Vitro Conversion of Propionate to Pyruvate by Salmonella enterica Enzymes: 2-Methylcitrate Dehydratase (PrpD) and Aconitase Enzymes Catalyze the Conversion of 2-Methylcitrate to 2-Methylisocitrate-Reference-Cited by-同舟云学术

In Vitro Conversion of Propionate to Pyruvate by Salmonella enterica Enzymes: 2-Methylcitrate Dehydratase (PrpD) and Aconitase Enzymes Catalyze the Conversion of 2-Methylcitrate to 2-Methylisocitrate

Published:2001-03-23 Issue:15 Volume:40 Page:4703-4713
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Horswill Alexander R.¹,Escalante-Semerena Jorge C.¹

Affiliation:

1. Department of Bacteriology, University of Wisconsin-Madison, 1550 Linden Drive, Madison Wisconsin 53706-1567

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi015503b

Reference50 articles.

1. Propionate catabolism in Salmonella typhimurium LT2: two divergently transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a member of the sigma-54 family of activators, and the prpBCDE genes constitute an operon

2. Salmonella typhimurium LT2 Catabolizes Propionate via the 2-Methylcitric Acid Cycle

3. Identification of D-threo-alpha-methylisocitrate as stereochemically specific substrate for bovine heart aconitase and inhibitor of TPN-linked isocitrate dehydrogenase.

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