BIOMAT Database Logo BIOMAT Database Logo

P-I class metalloproteinase from Bothrops moojeni venom is a post-proline cleaving peptidase with kininogenase activity: insights into substrate selectivity and kinetic behavior. 2014

Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.

Snake venom metalloproteinases (SVMPs) belonging to P-I class are able to hydrolyze extracellular matrix proteins and coagulation factors triggering local and systemic reactions by multiple molecular mechanisms that are not fully understood. BmooMPα-I, a P-I class SMVP from Bothrops moojeni venom, was active upon neuro- and vaso-active peptides including angiotensin I, bradykinin, neurotensin, oxytocin and substance P. Interestingly, BmooMPα-I showed a strong bias towards hydrolysis after proline residues, which is unusual for most of characterized peptidases. Moreover, the enzyme showed kininogenase activity similar to that observed in plasma and cells by kallikrein. FRET peptide assays indicated a relative promiscuity at its S2-S'2 subsites, with proline determining the scissile bond. This unusual post-proline cleaving activity was confirmed by the efficient hydrolysis of the synthetic combinatorial library MCA-GXXPXXQ-EDDnp, described as resistant for canonical peptidases, only after Pro residues. Structural analysis of the tripeptide LPL complexed with BmooMPα-I, generated by molecular dynamics simulations, assisted in defining the subsites and provided the structural basis for subsite preferences such as the restriction of basic residues at the S2 subsite due to repulsive electrostatic effects and the steric impediment for large aliphatic or aromatic side chains at the S1 subsite. These new functional and structural findings provided a further understanding of the molecular mechanisms governing the physiological effects of this important class of enzymes in envenomation process.

UI MeSH Term Description Entries
D007610 Kallikreins Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and hypotensives and increase vascular permeability and affect smooth muscle. They act as infertility agents in men. Three forms are recognized, PLASMA KALLIKREIN (EC 3.4.21.34), TISSUE KALLIKREIN (EC 3.4.21.35), and PROSTATE-SPECIFIC ANTIGEN (EC 3.4.21.77). Kallikrein,Kininogenase,Callicrein,Dilminal,Kallidinogenase,Kalliginogenase,Kallikrein A,Kallikrein B',Kallikrein Light Chain,Kinin-Forming Enzyme,Padutin,alpha-Kallikrein,beta-Kallikrein,beta-Kallikrein B,Enzyme, Kinin-Forming,Kinin Forming Enzyme,Light Chain, Kallikrein,alpha Kallikrein,beta Kallikrein,beta Kallikrein B
D007700 Kinetics The rate dynamics in chemical or physical systems.
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011863 Radioimmunoassay Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation. Radioimmunoassays
D003435 Crotalid Venoms Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized. Bothrops Venom,Crotalidae Venoms,Pit Viper Venoms,Rattlesnake Venoms,Crotactin,Crotalid Venom,Crotalin,Crotaline Snake Venom,Crotalotoxin,Crotamin,Pit Viper Venom,Rattlesnake Venom,Snake Venom, Crotaline,Venom, Bothrops,Venom, Crotalid,Venom, Crotaline Snake,Venom, Pit Viper,Venom, Rattlesnake,Venoms, Crotalid,Venoms, Crotalidae,Venoms, Pit Viper,Venoms, Rattlesnake,Viper Venom, Pit
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000085822 Prolyl Oligopeptidases A family of serine proteases with specificity for proline-specific cleavage of peptides that are not longer than 30 amino acids. In humans it is broadly distributed in all tissues with higher activity found in the brain. Post-Proline Cleaving Enzyme,Post-Proline Endopeptidase,Proline Endopeptidase,Proline Specific Endopeptidase,Prolyl Endopeptidase,Prolyl Endopeptidase (Thiol-dependent),Prolyl Endopeptidase I,Prolyl Oligopeptidase,Endopeptidase I, Prolyl,Endopeptidase, Post-Proline,Endopeptidase, Proline Specific,Oligopeptidases, Prolyl,Post Proline Cleaving Enzyme,Post Proline Endopeptidase
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012697 Serine Endopeptidases Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. Serine Endopeptidase,Endopeptidase, Serine,Endopeptidases, Serine

Related Publications

Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Rapid purification of a new P-I class metalloproteinase from Bothrops moojeni venom with antiplatelet activity.
January 2014, BioMed research international,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
A novel P-I class metalloproteinase with broad substrate-cleaving activity, agkislysin, from Agkistrodon acutus venom.
November 2004, Biochemical and biophysical research communications,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Biochemical, pharmacological and structural characterization of BmooMP-I, a new P-I metalloproteinase from Bothrops moojeni venom.
December 2020, Biochimie,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Bmoo FIBMP-I: A New Fibrinogenolytic Metalloproteinase from Bothrops moojeni Snake Venom.
January 2012, ISRN toxicology,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Structural studies of BmooMPalpha-I, a non-hemorrhagic metalloproteinase from Bothrops moojeni venom.
January 2010, Toxicon : official journal of the International Society on Toxinology,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom.
January 2009, Toxicon : official journal of the International Society on Toxinology,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Antiangiogenic properties of BthMP, a P-I metalloproteinase from Bothrops moojeni snake venom by VEGF pathway in endothelial cells.
April 2024, Biochemical and biophysical research communications,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Purification, crystallization and preliminary X-ray diffraction analysis of a class P-III metalloproteinase (BmMP-III) from the venom of Bothrops moojeni.
October 2012, Acta crystallographica. Section F, Structural biology and crystallization communications,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Isolation and characterization of moojenin, an acid-active, anticoagulant metalloproteinase from Bothrops moojeni venom.
December 2012, Toxicon : official journal of the International Society on Toxinology,
Débora N Okamoto, and Marcia Y Kondo, and Lilian C G Oliveira, and Rodrigo V Honorato, and Leticia M Zanphorlin, and Monika A Coronado, and Mariana S Araújo, and Guacyara da Motta, and Camila L Veronez, and Sheila S Andrade, and Paulo S L Oliveira, and Raghuvir K Arni, and Adelia C O Cintra, and Suely V Sampaio, and Maria A Juliano, and Luiz Juliano, and Mário T Murakami, and Iuri E Gouvea
Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom.
March 2008, Toxicon : official journal of the International Society on Toxinology,
Copied contents to your clipboard!