Molecular Basis of Dipeptide Recognition in <i>Drosophila melanogaster</i> Angiotensin I-Converting Enzyme Homologue, AnCE. [PDF]
Żukowska J+4 more
europepmc +1 more source
Diploid chromosome-level genome assembly and annotation for Lycorma delicatula. [PDF]
Snead AA+4 more
europepmc +1 more source
Effect of ACE mutations on blood ACE phenotype parameters. [PDF]
Kryukova OV+9 more
europepmc +1 more source
Nutritional value, antibacterial activity, ACE and DPP IV inhibitory of red pomegranate seeds protein and peptides. [PDF]
Akbarbaglu Z+5 more
europepmc +1 more source
Changes in Vertical Jump Parameters After Training Unit in Relation to <i>ACE</i>, <i>ACTN3</i>, <i>PPARA</i>, <i>HIF1A</i>, and <i>AMPD1</i> Gene Polymorphisms in Volleyball and Basketball Players. [PDF]
Vavak M+5 more
europepmc +1 more source
Bidirectional relation between dipeptidyl peptidase 4 and angiotensin II type I receptor signaling.
Martins FL+3 more
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Determination of peptidyl dipeptidase activity in 24 bacterial species
Of 24 bacterial species examined for lisinopril refractive peptidyl dipeptidase activity, only 8 contained activity. Activity in Pseudomonas maltophilia was more than fourfold higher than that of any other species. Pseudomonas maltophilia may be unique among bacteria in possessing high peptidyl dipeptidase activity that is both EDTA inhibitable and ...
Joanne Stevens+2 more
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Peptidyl dipeptidase in rabbit brain microvessels
The activity of peptidyl dipeptidase (peptidyldipeptide hydrolase, EC 3.4.15.1), also known as angiotensin-converting enzyme, was studied in small blood vessel preparations isolated from rabbit brain. The vascular preparation contained arterioles and capillaries and was essentially free of extravascular material.
Peter Brecher+3 more
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Peptidyl dipeptidase-4 from Pseudomonas maltophilia was modified with the arginine reagents p-hydroxyphenylglyoxal and 2,3-butanedione. The enzyme was inactivated in a pseudo-first-order manner by p-hydroxyphenylglyoxal with a half-time of 72 min. Inactivation by 2,3-butanedione was biphasic with a rapid phase followed by a slower inactivation to less ...
Joseph J. Lanzillo+2 more
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Peptidyl-dipeptidase A/angiotensin I-converting enzyme
Publisher Summary This chapter discusses the tissue distribution and the substrate specificity of peptidyl-dipeptidase A/angiotensin I-converting enzyme. Angiotensin I-Converting Enzyme (ACE) is a zinc metallopeptidase that belongs to the gluzincin family (clan MA) of metalloproteases of which thermolysin is the prototype.
Pierre Corvol+2 more
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