Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization,-Reference-Cited by-同舟云学术

Crystal Structure of a Hyperthermophilic Archaeal Acylphosphatase from Pyrococcus horikoshiiStructural Insights into Enzymatic Catalysis, Thermostability, and Dimerization,

Published:2005-03-01 Issue:12 Volume:44 Page:4601-4611
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cheung Yuk-Yin¹,Lam Sonia Y.¹,Chu Wai-Kit¹,Allen Mark D.¹,Bycroft Mark¹,Wong Kam-Bo¹

Affiliation:

1. Department of Biochemistry and Molecular Biotechnology Programme, The Chinese University of Hong Kong, Hong Kong, China, and MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, United Kingdom

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi047832k

Reference76 articles.

1. Acylphosphatase possesses nucleoside triphosphatase and nucleoside diphosphatase activities

2. The hydrolysis of 1,3-diphosphoglyceric acid by acyl phosphatase

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