Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily-Reference-Cited by-同舟云学术

Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily

Published:2017-03-01 Issue:3 Volume:30 Page:273-280
ISSN:1741-0126
Container-title:Protein Engineering, Design and Selection
language:en
Short-container-title:

Author:

Zahniser Megan P.D.¹,Prasad Shreenath²,Kneen Malea M.²,Kreinbring Cheryl A.¹³,Petsko Gregory A.¹³,Ringe Dagmar¹³⁴,McLeish Michael J.²

Affiliation:

1. Department of Biochemistry, Brandeis University, 415 South St., Waltham, MA 02454,USA

2. Department of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis (IUPUI), 402 N. Blackford Street, Indianapolis, IN 46202,USA

3. Rosenstiel Basic Medical Sciences Research Center, MS029, 415 South Street, Waltham, MA 02454,USA

4. Department of Chemistry, Brandeis University, 415 South St., Waltham, MA 02454,USA

Funder

National Science Foundation

Argonne National Laboratory

U.S. DOE

National Cancer Institute

National Institute of General Medical Sciences

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/30/3/273/14092465/gzx015.pdf

Reference53 articles.

1. Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase

2. The Protein Data Bank

3. Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenase

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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