1itq: Difference between revisions

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==Overview==

Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing, dipeptides and is involved in hydrolytic metabolism of penem and, carbapenem beta-lactam antibiotics. The crystal structures of the, saccharide-trimmed enzyme are determined as unliganded and, inhibitor-liganded forms. They are informative for designing new, antibiotics that are not hydrolyzed by this enzyme. The active site in, each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is, composed of binuclear zinc ions bridged by the Glu125 side-chain located, at the bottom of the barrel, and it faces toward the microvillar membrane, of a kidney tubule. A dipeptidyl moiety of the therapeutically used, cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The, barrel and active-site architectures utilizing catalytic metal ions, exhibit unexpected similarities to those of the murine adenosine deaminase, and the catalytic domain of the bacterial urease.

Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease.

==Disease==

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[[Category: zinc protease beta-lactamase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing, dipeptides and is involved in hydrolytic metabolism of penem and, carbapenem beta-lactam antibiotics. The crystal structures of the, saccharide-trimmed enzyme are determined as unliganded and, inhibitor-liganded forms. They are informative for designing new, antibiotics that are not hydrolyzed by this enzyme. The active site in, each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is, composed of binuclear zinc ions bridged by the Glu125 side-chain located, at the bottom of the barrel, and it faces toward the microvillar membrane, of a kidney tubule. A dipeptidyl moiety of the therapeutically used, cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The, barrel and active-site architectures utilizing catalytic metal ions, exhibit unexpected similarities to those of the murine adenosine deaminase, and the catalytic domain of the bacterial urease.
+Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme. The active site in each of the (alpha/beta)(8) barrel subunits of the homodimeric molecule is composed of binuclear zinc ions bridged by the Glu125 side-chain located at the bottom of the barrel, and it faces toward the microvillar membrane of a kidney tubule. A dipeptidyl moiety of the therapeutically used cilastatin inhibitor is fully accommodated in the active-site pocket, which is small enough for precise recognition of dipeptide substrates. The barrel and active-site architectures utilizing catalytic metal ions exhibit unexpected similarities to those of the murine adenosine deaminase and the catalytic domain of the bacterial urease.
 ==Disease==
@@ Line 30: / Line 30: @@
 [[Category: zinc protease beta-lactamase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:03:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:33 2008''