Membrane dipeptidase: Difference between revisions
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'''Membrane dipeptidase''' ({{EC number|3.4.13.19}}, ''renal dipeptidase'', ''dehydropeptidase I (DPH I)'', ''dipeptidase'', ''aminodipeptidase'', ''dipeptide hydrolase'', ''dipeptidyl hydrolase'', ''nonspecific dipeptidase'', ''glycosyl-phosphatidylinositol-anchored renal dipeptidase'', ''MDP'') is an [[enzyme]].<ref>{{cite journal | title = The purification and properties of a particulate renal dipeptidase |author = Campbell, B., Lin, H., Davis, R. and Ballew, E. |journal = Biochim. Biophys. Acta |date = 1966 |volume = 118 |pages = 371-386 |pmid = 5961612}}</ref><ref>{{cite journal | title = Renal dipeptidase |author = Campbell, B.J. |journal = Methods Enzymol. |date = 1970 |volume = 19 |pages = 722-729 |pmid = }}</ref><ref>{{cite journal | title = Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I |author = Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M. |journal = Antimicrob. Agents Chemother. |date = 1982 |volume = 22 |pages = 62-70 |pmid = 7125632}}</ref><ref>{{cite journal | title = Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme |author = Hooper, N.M., Keen, J.N. and Turner, A.J. |journal = Biochem. J. |date = 1990 |volume = 265 |pages = 429-433 |pmid = 2137335}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]] |
'''Membrane dipeptidase''' ({{EC number|3.4.13.19}}, ''renal dipeptidase'', ''dehydropeptidase I (DPH I)'', ''dipeptidase'', ''aminodipeptidase'', ''dipeptide hydrolase'', ''dipeptidyl hydrolase'', ''nonspecific dipeptidase'', ''glycosyl-phosphatidylinositol-anchored renal dipeptidase'', ''MDP'') is an [[enzyme]].<ref>{{cite journal | title = The purification and properties of a particulate renal dipeptidase |author = Campbell, B., Lin, H., Davis, R. and Ballew, E. |journal = Biochim. Biophys. Acta |date = 1966 |volume = 118 |pages = 371-386 |pmid = 5961612 |issue=2}}</ref><ref>{{cite journal | title = Renal dipeptidase |author = Campbell, B.J. |journal = Methods Enzymol. |date = 1970 |volume = 19 |pages = 722-729 |pmid = }}</ref><ref>{{cite journal | title = Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I |author = Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M. |journal = Antimicrob. Agents Chemother. |date = 1982 |volume = 22 |pages = 62-70 |pmid = 7125632 |issue=1}}</ref><ref>{{cite journal | title = Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme |author = Hooper, N.M., Keen, J.N. and Turner, A.J. |journal = Biochem. J. |date = 1990 |volume = 265 |pages = 429-433 |pmid = 2137335 |issue=2 |pmc=1136904}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]] |
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: [[Hydrolysis]] of [[dipeptides]] |
: [[Hydrolysis]] of [[dipeptides]] |
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Revision as of 21:36, 1 November 2013
| Membrane dipeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.13.19 | ||||||||
| CAS no. | 9031-99-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Membrane dipeptidase (EC 3.4.13.19, renal dipeptidase, dehydropeptidase I (DPH I), dipeptidase, aminodipeptidase, dipeptide hydrolase, dipeptidyl hydrolase, nonspecific dipeptidase, glycosyl-phosphatidylinositol-anchored renal dipeptidase, MDP) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
This membrane-bound, zinc enzyme has broad specificity.
References
- ^ Campbell, B., Lin, H., Davis, R. and Ballew, E. (1966). "The purification and properties of a particulate renal dipeptidase". Biochim. Biophys. Acta. 118 (2): 371–386. PMID 5961612.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Campbell, B.J. (1970). "Renal dipeptidase". Methods Enzymol. 19: 722–729.
- ^ Kropp, H., Sundelof, J.G., Hajdu, R. and Kahan, F.M. (1982). "Metabolism of thienamycin and related carbapenem antibiotics by renal dipeptidase, dehydropeptidase-I". Antimicrob. Agents Chemother. 22 (1): 62–70. PMID 7125632.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Hooper, N.M., Keen, J.N. and Turner, A.J. (1990). "Characterization of the glycosyl-phosphatidylinositol-anchored human renal dipeptidase reveals that it is more extensively glycosylated than the pig enzyme". Biochem. J. 265 (2): 429–433. PMC 1136904. PMID 2137335.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Membrane+dipeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)