Results 11 to 20 of about 4,028 (99)
Endopeptidase-24.5 is not a metallo-endopeptidase [PDF]
Biochemical Journal, 1987 Judith Bond, P. Elaine Butler
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Journal of Biological Chemistry, 1995 A peptidase, isolated from rat testes, is inhibited by 1 mM o-phenanthroline, 1 microM N-(1-(R,S)-carboxyl-3-phenylpropyl)-Ala-Ala-Phe-p-aminobenzoate, and 6 mM Pro-Ile, properties similar to those ascribed to endopeptidase 24.16. The enzyme hydrolyzes dynorphin A-8, neurotensin 1-13, angiotensin I, and substance P.
Louis B. Hersh, Donald Rodd
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Macrocyclization by asparaginyl endopeptidases [PDF]
New Phytologist, 2017 Contents Summary 923 I. Introduction 923 II. Plant AEPs with macrocyclizing ability 924 III. Mechanism of macrocyclization by AEPs 925 IV. Conclusions 927 Acknowledgements 927 References 927 SummaryPlant asparaginyl endopeptidases (AEPs) are important for the post‐translational processing of seed storage proteins via ...
Amy M. James +2 more
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Specificity of prolyl endopeptidase [PDF]
FEBS Letters, 1986 A series of tetrapeptides, Cbz(Bz)‐Gly‐X‐Leu‐Gly, were synthesized and the kinetic parameters, k cat and , determined for their hydrolyses by prolyl endopeptidase from Flavobacterium. The peptides with X = N‐Me‐Ala, Sar and Ala as well as the standard substrate (X = Pro) were found to be good substrates, while those with X = α‐aminobutyryl, Hyp, Ser ...
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Endopeptidases and prohormone processing
Bioscience Reports, 1990 Peptide hormones and peptide transmitters are generated from polypeptide precursors by specific cleavage reactions which take place principally at sites formed by single or paired basic residues. Not all the possible cleavage sites are utilised, however, and the degree of processing of many propeptides has been found to vary according to the tissue of ...
Nigel J. Darby, D. G. Smyth
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Staurosporine, a Prolyl Endopeptidase Inhibitor [PDF]
Agricultural and Biological Chemistry, 1990 (1990). Staurosporine, a Prolyl Endopeptidase Inhibitor. Agricultural and Biological Chemistry: Vol. 54, No. 11, pp. 3021-3022.
Ken-ichi Kimura +3 more
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Hydrolysis of rat melanin-concentrating hormone by endopeptidase 24.11 (neutral endopeptidase) [PDF]
Biochemical Journal, 1992 Melanin-concentrating hormone (MCH) is a cyclic peptide which behaves as an antagonist of the pituitary melanotropic hormone alpha-melanocyte-stimulating hormone in fishes. Cloning of the rat MCH cDNA precursor recently revealed the presence of an additional putative peptide named NEI.
Jean-Pierre Vincent +4 more
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Peptide Cross-Links in Bacterial Cell Wall Peptidoglycans Studied with Specific Endopeptidases from Streptomyces albus G [PDF]
, 1966 Jean‐François Petit +2 more
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Purification and Characterization of Vicilin Peptidohydrolase, the Major Endopeptidase in the Cotyledons of Mung‐Bean Seedlings [PDF]
, 1977 Bruno Baumgartner, Maarten J. Chrispeels
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Relationship between lysostaphin endopeptidase production and cell wall composition in Staphylococcus staphylolyticus [PDF]
, 1979 John M. Robinson +2 more
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