Male fertility is dependent on dipeptidase activity of testis ACE.

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Publication Type Journal Article
School or College School of Medicine; College of Science
Department Oncological Sciences; Biology; Human Genetics
Program Institute of Human Genetics; Howard Hughes Medical Institute (HHMI)
Creator Capecchi, Mario R.
Other Author Fuchs, Sebastien; Frenzel, Kristen; Hubert, Christine; Lyng, Robert; Muller, Laurent; Michaud, Annie; Xiao, Hong D.; Adams, Jonathan W.; Corvol, Pierre; Shur, Barry D.; Bernstein, Kenneth E
Title Male fertility is dependent on dipeptidase activity of testis ACE.
Date 2005-11-11
Description Testis angiotensin-converting enzyme (ACE) is an isozyme exclusively expressed by developing sperm. This protein has only a single catalytic domain containing the HEXXH consensus-site motif typical of zinc metallopeptidases. The exact role of testis ACE is unknown, but male mice lacking the protein reproduce poorly, despite normal numbers of sperm and normal motility.
Type Text
Publisher Nature Publishing Group
Volume 11
Issue 11
First Page 1140
Last Page 1142
Subject Amino Acid Motifs; Blotting, Western; Catalytic Domain; Comparative Study; Isoenzymes; Protein Structure, Tertiary
Subject MESH Fertility; Peptidyl-Dipeptidase A; Testis
Language eng
Bibliographic Citation Nat Med. 2005 Nov;11(11):1140-2; author reply 1142-3. Fuchs S, Frenzel K, Hubert C, Lyng R, Muller L, Michaud A, Xiao HD, Adams JW, Capecchi MR, Corvol P, Shur BD, Bernstein KE. Male fertility is dependent on dipeptidase activity of testis ACE. Retrieved on November 2, 2006 from http://www.nature.com/nm/journal/v11/n11/abs/nm1105-1140.html.
Rights Management copyright ? 2005 Nature Publishing Group. All Rights Reserved.
Format Medium application/pdf
Identifier ir-main,556
ARK ark:/87278/s6t44bg8
Setname ir_uspace
ID 704793
Reference URL https://collections.lib.utah.edu/ark:/87278/s6t44bg8