| pubmed-article:11815627 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11815627 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11815627 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:11815627 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:11815627 | lifeskim:mentions | umls-concept:C0960880 | lld:lifeskim |
| pubmed-article:11815627 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:11815627 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:11815627 | pubmed:dateCreated | 2002-4-22 | lld:pubmed |
| pubmed-article:11815627 | pubmed:abstractText | Human angiotensin-converting enzyme-related carboxypeptidase (ACE2) is a zinc metalloprotease whose closest homolog is angiotensin I-converting enzyme. To begin to elucidate the physiological role of ACE2, ACE2 was purified, and its catalytic activity was characterized. ACE2 proteolytic activity has a pH optimum of 6.5 and is enhanced by monovalent anions, which is consistent with the activity of ACE. ACE2 activity is increased approximately 10-fold by Cl(-) and F(-) but is unaffected by Br(-). ACE2 was screened for hydrolytic activity against a panel of 126 biological peptides, using liquid chromatography-mass spectrometry detection. Eleven of the peptides were hydrolyzed by ACE2, and in each case, the proteolytic activity resulted in removal of the C-terminal residue only. ACE2 hydrolyzes three of the peptides with high catalytic efficiency: angiotensin II () (k(cat)/K(m) = 1.9 x 10(6) m(-1) s(-1)), apelin-13 (k(cat)/K(m) = 2.1 x 10(6) m(-1) s(-1)), and dynorphin A 1-13 (k(cat)/K(m) = 3.1 x 10(6) m(-1) s(-1)). The ACE2 catalytic efficiency is 400-fold higher with angiotensin II () as a substrate than with angiotensin I (). ACE2 also efficiently hydrolyzes des-Arg(9)-bradykinin (k(cat)/K(m) = 1.3 x 10(5) m(-1) s(-1)), but it does not hydrolyze bradykinin. An alignment of the ACE2 peptide substrates reveals a consensus sequence of: Pro-X((1-3 residues))-Pro-Hydrophobic, where hydrolysis occurs between proline and the hydrophobic amino acid. | lld:pubmed |
| pubmed-article:11815627 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11815627 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11815627 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11815627 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11815627 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11815627 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:KnabWW | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:GavinJamesJ | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:VickersChadC | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:HalesPaulP | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:KaushikVirend... | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:DickLarryL | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:TangJinJ | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:GodboutKevinK | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:ParsonsThomas... | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:BaronasElizab... | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:ActonSusanS | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:PataneMichael... | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:NicholsAndrew... | lld:pubmed |
| pubmed-article:11815627 | pubmed:author | pubmed-author:TumminoPeterP | lld:pubmed |
| pubmed-article:11815627 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11815627 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:11815627 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11815627 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11815627 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11815627 | pubmed:pagination | 14838-43 | lld:pubmed |
| pubmed-article:11815627 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11815627 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11815627 | pubmed:articleTitle | Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. | lld:pubmed |
| pubmed-article:11815627 | pubmed:affiliation | Department of Metabolic Disease, Millennium Pharmaceuticals, Inc., Cambridge, Massachusetts 02139, USA. | lld:pubmed |
| pubmed-article:11815627 | pubmed:publicationType | Journal Article | lld:pubmed |
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