Allosteric Activation and Contrasting Properties of l-Serine Dehydratase Types 1 and 2-Reference-Cited by-同舟云学术

Allosteric Activation and Contrasting Properties of l-Serine Dehydratase Types 1 and 2

Published:2012-06-20 Issue:26 Volume:51 Page:5320-5328
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chen Shawei¹,Xu Xiao Lan¹,Grant Gregory A.¹

Affiliation:

1. Department of Developmental Biology and ‡Department of Medicine, Washington University School of Medicine, 660 South Euclid Avenue, Box 8103, St. Louis, Missouri 63110, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300523p

Reference22 articles.

1. Aconitase as Iron−Sulfur Protein, Enzyme, and Iron-Regulatory Protein

2. Iron−Sulfur Proteins with Nonredox Functions

3. Bacterial l-serine dehydratases: a new family of enzymes containing iron-sulfur clusters

4. Purification and properties of an iron-sulfur-containing and pyridoxal-phosphate-independent l-Serine dehydratase from Peptostreptococcus asaccharolyticus

5. Iron-sulfur cluster-containingl-serine dehydratase fromPeptostreptococcus asaccharolyticus: Correlation of the cluster type with enzymatic activity

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