Enzymes
| UniProtKB help_outline | 1,732 proteins |
Reaction participants Show >> << Hide
- Name help_outline Leu-enkephalin Identifier CHEBI:190689 Charge 0 Formula C28H37N5O7 InChIKeyhelp_outline URLZCHNOLZSCCA-VABKMULXSA-N SMILEShelp_outline CC(C)C[C@H](NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)CNC(=O)CNC(=O)[C@@H]([NH3+])CC1=CC=C(O)C=C1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-tyrosylglycylglycine Identifier CHEBI:190708 Charge 0 Formula C13H17N3O5 InChIKeyhelp_outline HIINQLBHPIQYHN-JTQLQIEISA-N SMILEShelp_outline [NH3+][C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(=O)NCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-phenylalanyl-L-leucine Identifier CHEBI:190710 Charge 0 Formula C15H22N2O3 InChIKeyhelp_outline RFCVXVPWSPOMFJ-STQMWFEESA-N SMILEShelp_outline CC(C)C[C@H](NC(=O)[C@@H]([NH3+])CC1=CC=CC=C1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:71487 | RHEA:71488 | RHEA:71489 | RHEA:71490 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
-
Purification and characterization of human converting enzyme (kininase II).
Stewart T.A., Weare J.A., Erdoes E.G.
We purified peptidyl-dipeptidase (converting enzyme, EC 3.4.15.1) to homogeneity from the membrane fraction of human lung and for comparison, from human and hog kidney. The membrane-bound lung enzyme was purified 1800-fold with 19% yield, and the kidney enzyme 640-fold with 10% yield. The specific ... >> More
We purified peptidyl-dipeptidase (converting enzyme, EC 3.4.15.1) to homogeneity from the membrane fraction of human lung and for comparison, from human and hog kidney. The membrane-bound lung enzyme was purified 1800-fold with 19% yield, and the kidney enzyme 640-fold with 10% yield. The specific activities with Bz-Gly-His-Leu were 81 mumol/min/mg for the lung and 65 for the kidney enzyme. The lung enzyme was homogeneous in gel electrophoresis with Mr = 155,000 and Sw,20 = 8.0 in ultracentrifugation. Antibodies elicited against lung or kidney enzyme cross-reacted with enzyme from other organ, but not with the hog enzyme. In isoelectric focusing both human enzymes had a major form with a pI of 5.2. The lung preparation also contained more acidic forms (pI = 4--5), which were eliminated by treatment with neuraminidase. Lung and kidney converting enzyme hydrolyzed bradykinin, angiotensin I, and enkephalins and had similar kinetic constants. Bradykinin was the best substrate, as indicated by its kcat/Km, but Met5-enkephalin had the highest turnover number. The hydrolysis of Bz-Gly-His-Leu was inhibited by captopril (SQ 14225) competitively, and by Keto-ACE, a non-peptide derivative of Bz-Phe-Gly-Pro, non-competitively. << Less
Peptides 2:145-152(1981) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
-
Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase.
Erdoes E.G., Johnson A.R., Boyden N.T.
Biochem. Pharmacol. 27:843-848(1978) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.