Results 11 to 20 of about 265,113 (235)

Substrate specificity of honeydew melon protease D, a plant serine endopeptidase. [PDF]

open access: yesBioscience, Biotechnology, and Biochemistry, 1997
The substrate specificity of honeydew melon (Cucumis melo var. inodorus Naud) protease D was studied by the use of synthetic substrates and oligopeptides derived from a protein hydrolyzate. The hydrolysis rates of succinyl-(L-Ala)1-3-p-nitroanilide (Suc-(Ala)1-3-pNA) the hydrolysis rate progressively rose in proportion to the increased chain length ...
H. Yonezawa, T. Uchikoba, M. Kaneda
semanticscholar   +3 more sources

Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots. [PDF]

open access: yesBiochemical Journal, 1996
An endopeptidase (designated RSIP, for root-starvation-induced protease) was purified to homogeneity from glucose-starved maize roots. The molecular mass of the enzyme was 59 kDa by SDS/PAGE under reducing conditions and 62 kDa by gel filtration on a Sephacryl S-200 column. The isoelectric point of RSIP was 4.55. The purified enzyme was stable, with no
F. James   +4 more
semanticscholar   +5 more sources

High-level production of Aspergillus niger prolyl endopeptidase from agricultural residue and its application in beer brewing

open access: yesMicrobial Cell Factories, 2023
Background Prolyl endopeptidase from Aspergillus niger (AN-PEP) is a prominent serine proteinase with various potential applications in the food and pharmaceutical industries. However, the availability of efficient and low-cost AN-PEP remains a challenge
Minglu Liu   +4 more
doaj   +2 more sources

Analysis of a Lys-specific serine endopeptidase secreted via the type IX secretion system in Porphyromonas gingivalis. [PDF]

open access: yesFEMS Microbiology Letters, 2014
Porphyromonas gingivalis, a significant causative agent of adult periodontitis, possesses a novel secretion system called the type IX secretion system (T9SS). A number of virulence factors, such as Arg-gingipain (Rgp), are translocated onto the cell surface and into the extracellular milieu via the T9SS. In this study, we found that the PGN_1416 90- to
Minako Nonaka   +6 more
semanticscholar   +3 more sources

A human serine endopeptidase, purified with respect to activity against a peptide with phosphoserine in the P1' position, is apparently identical with prolyl endopeptidase.

open access: yesJournal of Biological Chemistry, 1991
The present work describes the detection, purification, and characterization of a serine endopeptidase with preference for a phosphoserine in the P1' position of the substrate. During probing for the enzyme in crude extracts, as well as during its 64,000-
J. Rosen   +3 more
semanticscholar   +3 more sources

SmSP2: A serine protease secreted by the blood fluke pathogen Schistosoma mansoni with anti-hemostatic properties. [PDF]

open access: yesPLoS Neglected Tropical Diseases, 2018
BACKGROUND:Serine proteases are important virulence factors for many pathogens. Recently, we discovered a group of trypsin-like serine proteases with domain organization unique to flatworm parasites and containing a thrombospondin type 1 repeat (TSR-1 ...
Adrian Leontovyč   +13 more
doaj   +6 more sources

Prolyl endopeptidase-like is a (thio)esterase involved in mitochondrial respiratory chain function

open access: yesiScience, 2021
Summary: Deficiency of the serine hydrolase prolyl endopeptidase-like (PREPL) causes a recessive metabolic disorder characterized by neonatal hypotonia, feeding difficulties, and growth hormone deficiency.
Karen Rosier   +21 more
doaj   +2 more sources

Sensitive substrates for neprilysin (neutral endopeptidase) and thermolysin that are highly resistant to serine proteases [PDF]

open access: yesFEBS Letters, 1996
Tripeptide derivatives like 3‐carboxypropanoylalanyl‐alanyl‐leucine 4‐nitroanilide or 3‐carboxypropanoylalanyl‐alanyl‐phenylalanine 4‐nitroanilide are very sensitive substrates for neprilysin (k cat > 102 s−1; k cat/K m ≥ 106 s−1 · M−1) and are widely employed in investigations of the enzyme. However, these compounds are also good substrates for the
Shmuel Carmeli, Shmaryahu Blumberg
exaly   +3 more sources

Safety evaluation of the food enzyme subtilisin from the genetically modified Bacillus paralicheniformis strain AP‐GKY [PDF]

open access: yesEFSA Journal
The food enzyme subtilisin (serine endopeptidase; EC 3.4.21.62) is produced with the genetically modified Bacillus paralicheniformis strain AP‐GKY by Kerry Ingredients & Flavours Ltd.
EFSA Panel on Food Enzymes (FEZ)   +16 more
doaj   +2 more sources

Isolation and Characterization of a Highly Specific Serine Endopeptidase from an Oral Strain of Staphylococcus epidermidis

open access: yesBiological Chemistry, 2001
Infection by Staphylococcus epidermidis, an opportunistic pathogen, has become a major problem due to the increased use of implanted medical devices and the growing number of patients who are therapeutically or infectiously immunosuppressed. These infections appear to proceed via modulation of the coagulation and complement systems.
J. Moon   +4 more
semanticscholar   +4 more sources

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