Mammalian Alkaline Phosphatase Catalysis Requires Active Site Structure Stabilization via the N-Terminal Amino Acid Microenvironment-Reference-Cited by-同舟云学术

Mammalian Alkaline Phosphatase Catalysis Requires Active Site Structure Stabilization via the N-Terminal Amino Acid Microenvironment

Published:2006-07-25 Issue:32 Volume:45 Page:9756-9766
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hoylaerts Marc F.¹,Ding Lan¹,Narisawa Sonoko¹,Van kerckhoven Soetkin¹,Millán José Luis¹

Affiliation:

1. Burnham Institute for Medical Research, La Jolla, California 92037, and Center for Molecular and Vascular Biology, University of Leuven, Leuven, Belgium

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi052471%2B

Reference29 articles.

1. Alkaline Phosphatase

2. Millán, J. L. (2006)Mammalian alkaline phosphatases. From biology to applications in medicine and biotechnology, pp 1−322, Wiley-VCH Verlag GmbH & Co., Weinheim, Germany.

3. Gly429 is the major determinant of uncompetitive inhibition of human germ cell alkaline phosphatase by l-leucine

4. Site-directed mutagenesis and epitope-mapped monoclonal antibodies define a catalytically important conformational difference between human placental and germ cell alkaline phosphatase

5. Molecular mechanism of uncompetitive inhibition of human placental and germ-cell alkaline phosphatase

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