N-Tosyl-l-phenylalanine Chloromethyl Ketone, a Serine Protease Inhibitor, Identifies Glutamate 398 at the Coenzyme-Binding Site of Human Aldehyde Dehydrogenase. Evidence for a Second “Naked Anion” at the Active Site-Reference-Cited by-同舟云学术

N-Tosyl-l-phenylalanine Chloromethyl Ketone, a Serine Protease Inhibitor, Identifies Glutamate 398 at the Coenzyme-Binding Site of Human Aldehyde Dehydrogenase. Evidence for a Second “Naked Anion” at the Active Site

Published:1998-09-17 Issue:40 Volume:37 Page:14151-14156
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dryjanski Marek¹,Kosley Lynda L.¹,Pietruszko Regina¹

Affiliation:

1. Center of Alcohol Studies, Rutgers The State University of New Jersey, 607 Allison Road, Piscataway, New Jersey 08854-8001

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi981278v

Reference33 articles.

1. Jakoby, W. B. (1963) inThe Enzymes(Boyer, P. D., Ed.) Vol. 7, pp 203−219.

2. Selective chemical modification of human liver aldehyde dehydrogenases E1 and E2 by iodoacetamide.

3. 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

4. Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone

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