Dipeptidyl peptidase IV, a kidney brush-border serine peptidase [PDF]
Biochemical Journal, 1976 Dipeptidyl peptidase IV, an enzyme that releases dipeptides from substrates with N-terminal sequences of the forms X-Pro-Y or X-Ala-Y, was purified 300-fold from pig kidney cortex. The kidney is the main source of the enzyme, where it is one of the major microvillus-membrane proteins.
A J, Kenny +6 more
openaire +2 more sources
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source
FEBS Letters, EarlyView.This study reveals a unique active site enriched in methionine residues and demonstrates that these residues play a critical role by stabilizing carbocation intermediates through novel sulfur–cation interactions. Structure‐guided mutagenesis further revealed variants with significantly altered product profiles, enhancing pseudopterosin formation. These
Marion Ringel +13 more
wiley +1 more source
Matrix processing peptidase of mitochondria [PDF]
, 1990 The mitochondrial processing peptidase (MPP) and the processing enhancing protein (PEP) cooperate in the proteolytic cleavage of matrix targeting sequences from nuclear-encoded mitochondrial precursor proteins.
Arretz, Michael +3 more
core
Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
FEBS Letters, EarlyView.Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz +11 more
wiley +1 more source
Proteomic analysis of human skin treated with larval schistosome peptidases reveals distinct invasion strategies among species of blood flukes. [PDF]
PLoS Neglected Tropical Diseases, 2011 Skin invasion is the initial step in infection of the human host by schistosome blood flukes. Schistosome larvae have the remarkable ability to overcome the physical and biochemical barriers present in skin in the absence of any mechanical trauma.
Jessica Ingram +5 more
doaj +1 more source
Substrate specificity and structural investigation into PepO and PepW : two peptidases from Lactobacillus rhamnosus : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University, Palmerston North, New Zealand [PDF]
, 2005 The proteolytic systems of lactic acid bacteria have important roles in the maturation and flavour development of cheese. Lactic acid bacteria pepetidases contribute to the taste of cheese through the production of low-molecular weight peptides and free ...
Yates, Karen Maree
core
Biogenesis of mitochondrial c-type cytochromes [PDF]
, 1990 Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
core +2 more sources
An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
The processing peptidase of yeast mitochondria [PDF]
, 1988 Two proteins co-operate in the proteolytic cleavage of mitochondrial precursor proteins: the mitochondrial processing peptidase (MPP) and the processing enhancing protein (PEP).
Cheng, Ming Yuan +5 more
core