PMID: 12144777

 

    Legend: Gene, Sites

Title : Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis

Abstract :

1. Human renal dipeptidase is a membrane-bound glycoprotein hydrolyzing dipeptides and is involved in hydrolytic metabolism of penem and carbapenem beta-lactam antibiotics
2. The crystal structures of the saccharide-trimmed enzyme are determined as unliganded and inhibitor-liganded forms
3. They are informative for designing new antibiotics that are not hydrolyzed by this enzyme
4. 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
5. 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
6. 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

Output (sent_index, trigger, protein, sugar, site):

• 1. glycoprotein, , glycoprotein, -, -
• 1. glycoprotein, , renal dipeptidase, -, -

Output(Part-Of) (sent_index, protein, site):

• 4. subunits, site
• 6. urease, domain

*Output_Site_Fusion* (sent_index, protein, sugar, site):

 

Protein	NCBI ID	SENTENCE INDEX
adenosine deaminase	11486	6