Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15

Carol Rosenbaum; Christopher Cardozo; Marvin Lesser

doi:10.1016/0196-9781(95)00006-6

Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15

Carol Rosenbaum, Christopher Cardozo, Marvin Lesser

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10 Scopus citations

Abstract

Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in tissues. EP 24.11 cleaved LBK at the Gly⁵-Phe⁶ and Pro⁸-Phe⁹ bonds, whereas EP 24.15 cleaved the Phe⁶-Ser⁷ bond. Determination of kinetic constants for degradation of LBK by the two enzymes yielded k_cat K_m ratios of 5.2 × 10⁵ and 8.4 × 10⁵ for EP 24.15 and EP 24.11, respectively, indicating that LBK is a good substrate for both enzymes. The findings demonstrate that both EP 24.11 and EP 24.15 efficiently degrade LBK and thus may contribute to the inactivation of this peptide in tissues.

Original language	English
Pages (from-to)	523-525
Number of pages	3
Journal	Peptides
Volume	16
Issue number	3
DOIs	https://doi.org/10.1016/0196-9781(95)00006-6
State	Published - 1995

Keywords

Bradykinin
Degradation
Endopeptidase 24.11
Endopeptidase 24.15
Lysylbradykinin

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10.1016/0196-9781(95)00006-6

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title = "Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15",

abstract = "Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in tissues. EP 24.11 cleaved LBK at the Gly5-Phe6 and Pro8-Phe9 bonds, whereas EP 24.15 cleaved the Phe6-Ser7 bond. Determination of kinetic constants for degradation of LBK by the two enzymes yielded kcat Km ratios of 5.2 × 105 and 8.4 × 105 for EP 24.15 and EP 24.11, respectively, indicating that LBK is a good substrate for both enzymes. The findings demonstrate that both EP 24.11 and EP 24.15 efficiently degrade LBK and thus may contribute to the inactivation of this peptide in tissues.",

keywords = "Bradykinin, Degradation, Endopeptidase 24.11, Endopeptidase 24.15, Lysylbradykinin",

author = "Carol Rosenbaum and Christopher Cardozo and Marvin Lesser",

year = "1995",

doi = "10.1016/0196-9781(95)00006-6",

language = "English",

volume = "16",

pages = "523--525",

journal = "Peptides",

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publisher = "Elsevier Inc.",

number = "3",

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TY - JOUR

T1 - Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15

AU - Rosenbaum, Carol

AU - Cardozo, Christopher

AU - Lesser, Marvin

PY - 1995

Y1 - 1995

N2 - Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in tissues. EP 24.11 cleaved LBK at the Gly5-Phe6 and Pro8-Phe9 bonds, whereas EP 24.15 cleaved the Phe6-Ser7 bond. Determination of kinetic constants for degradation of LBK by the two enzymes yielded kcat Km ratios of 5.2 × 105 and 8.4 × 105 for EP 24.15 and EP 24.11, respectively, indicating that LBK is a good substrate for both enzymes. The findings demonstrate that both EP 24.11 and EP 24.15 efficiently degrade LBK and thus may contribute to the inactivation of this peptide in tissues.

AB - Lysylbradykinin (LBK), a potent bioactive peptide with pleiotropic actions, is the major kinin generated in the extravascular space. To explore possible mechanisms of inactivation of this peptide in tissues, we evaluated its degradation by endopeptidase 24.11 (EP 24.11) and endopeptidase 24.15 (EP 24.15), two zinc metalloenzymes widely distributed in tissues. EP 24.11 cleaved LBK at the Gly5-Phe6 and Pro8-Phe9 bonds, whereas EP 24.15 cleaved the Phe6-Ser7 bond. Determination of kinetic constants for degradation of LBK by the two enzymes yielded kcat Km ratios of 5.2 × 105 and 8.4 × 105 for EP 24.15 and EP 24.11, respectively, indicating that LBK is a good substrate for both enzymes. The findings demonstrate that both EP 24.11 and EP 24.15 efficiently degrade LBK and thus may contribute to the inactivation of this peptide in tissues.

KW - Bradykinin

KW - Degradation

KW - Endopeptidase 24.11

KW - Endopeptidase 24.15

KW - Lysylbradykinin

UR - http://www.scopus.com/inward/record.url?scp=0029039850&partnerID=8YFLogxK

U2 - 10.1016/0196-9781(95)00006-6

DO - 10.1016/0196-9781(95)00006-6

M3 - Article

C2 - 7651908

AN - SCOPUS:0029039850

SN - 0196-9781

VL - 16

SP - 523

EP - 525

JO - Peptides

JF - Peptides

IS - 3

ER -

Degradation of lysylbradykinin by endopeptidase 24.11 and endopeptidase 24.15

Abstract

Keywords

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