Results 21 to 30 of about 23,292 (261)

Aminopeptidase C of Aspergillus niger is a Novel Phenylalanine Aminopeptidase [PDF]

open access: yes, 2003
A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share ...
Basten, E.J.W.   +2 more
core   +2 more sources

Prodrugs Activated by Vascular Ectopeptidases: Proof of Concept

open access: yesMedical Sciences Forum, 2022
Several vascular ectopeptidases reside in blood vessels and efficiently regulate peptide hormones. For instance, bradykinin (BK) is inactivated by angiotensin converting enzyme (ACE) or arginine-carboxypeptidases (Arg-CPs), and aminopeptidase N (APN ...
François Marceau
doaj   +1 more source

Selective Cytotoxicity of Carboxypeptidase-activated Methotrexate ex-Peptides

open access: yesPteridines, 1989
Methotrexate ex-pep tides (derivatives in which an amino acid is linked covalently to the ex-carboxyl of the glutamate residue on the parent drug) can be hydrolyzed by specific carboxypeptidases to yield free Methotrexate (MTX) and the corresponding ...
Vitols Karin S.   +3 more
doaj   +1 more source

Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. [PDF]

open access: yesPLoS ONE, 2014
Beta-lactam antibiotics target penicillin-binding proteins including several enzyme classes essential for bacterial cell-wall homeostasis. To better understand the functional and inhibitor-binding specificities of penicillin-binding proteins from the ...
Daniil M Prigozhin   +8 more
doaj   +1 more source

Peptide inhibitors of Streptomyces DD-carboxypeptidases [PDF]

open access: yes, 1973
1. Peptides that inhibit the dd-carboxypeptidases from Streptomyces strains albus G and R61 were synthesized. They are close analogues of the substrates of these enzymes.
Frère, Jean-Marie   +4 more
core   +1 more source

Cryo-EM structure of VASH1-SVBP bound to microtubules

open access: yeseLife, 2020
The dynamic tyrosination-detyrosination cycle of α-tubulin regulates microtubule functions. Perturbation of this cycle impairs mitosis, neural physiology, and cardiomyocyte contraction.
Faxiang Li   +7 more
doaj   +1 more source

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases [PDF]

open access: yes, 2011
Phytocystatins are inhibitors of cysteine-proteases from plants putatively involved in plant defence based on their capability of inhibit heterologous enzymes.
A Kiggundu   +49 more
core   +2 more sources

D-Arg0-Bradykinin-Arg-Arg, a Latent Vasoactive Bradykinin B2 Receptor Agonist Metabolically Activated by Carboxypeptidases

open access: yesFrontiers in Pharmacology, 2018
We previously reported hypotensive and vasodilator effects from C-terminally extended bradykinin (BK) sequences that behave as B2 receptor (B2R) agonists activated by vascular or plasma peptidases.
Hélène Bachelard   +2 more
doaj   +1 more source

High expression of human carboxypeptidase M in Pichia pastoris. Purification and partial characterization [PDF]

open access: yes, 2006
Carboxypeptidase M (CPM) is an extracellular glycosylphosphatidylinositol-anchored membrane glycoprotein, which removes the C-terminal basic residues, lysine and arginine, from peptides and proteins at neutral pH.
Araujo, Ronaldo Carvalho [UNIFESP]   +7 more
core   +1 more source

Proteome-derived Peptide Libraries to Study the Substrate Specificity Profiles of Carboxypeptidases*

open access: yesMolecular & Cellular Proteomics, 2013
Through processing peptide and protein C termini, carboxypeptidases participate in the regulation of various biological processes. Few tools are however available to study the substrate specificity profiles of these enzymes.
S. Tanco   +7 more
semanticscholar   +1 more source

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