Results 11 to 20 of about 25,546 (199)
The subtilase family (S8), a member of the clan SB of serine proteases are ubiquitous in all kingdoms of life and fulfil different physiological functions.
Fabian Falkenberg +3 more
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Interaction of subtilisins with serpins [PDF]
AbstractSerpins are well‐characterized inhibitors of the chymotrypsin family serine proteinases. We have investigated the interaction of two serpins with members of the subtilisin family, proteinases that possess a similar catalytic mechanism to the chymotrypsins, but a totally different scaffold.
T, Komiyama +3 more
openaire +2 more sources
Proteases, catalysing protein hydrolysis, and arylsulfatases, catalysing sulfate-ester hydrolysis, are key microbial enzymes for N and S mineralization in soil.
Nicolas Romillac +3 more
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Treatment of wool fibres with subtilisin and subtilisin-PEG [PDF]
Abstract In this work the diffusion of serine proteases into wool fabrics and yarns was studied. The proteases used were free subtilisin and subtilisin-PEG (the same enzyme that was covalently cross linked to polyethylene glycol). It is shown that the adsorption and diffusion is facilitated by the pre-treatment performed, being the alkaline ...
Silva, Carla J. S. M. +3 more
openaire +2 more sources
Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis
The cell envelope proteinase (CEP) of Lactococcus lactis is a large extracellular protease covalently linked to the peptidoglycan of the cell wall. Strains of L.
Egon Bech Hansen, Paolo Marcatili
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Subtilisin proteases, found in all organisms, are enzymes important in the post-translational steps of protein processing. In Leishmania major and L. donovani, this enzyme has been described as essential to their survival; however, few compounds that ...
Pollyanna Stephanie Gomes +12 more
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Dependence receptor involvement in subtilisin-induced long-term depression and in long-term potentiation [PDF]
The serine protease subtilisin induces a form of long-term depression (LTD) which is accompanied by a reduced expression of the axo-dendritic guidance molecule Unco-ordinated-5C (Unc-5C).
Darlington, L. Gail +2 more
core +1 more source
The recent identification of catalytically active peptidylglycine α-amidating monooxygenase (PAM) in Chlamydomonas reinhardtii, a unicellular green alga, suggested the presence of a PAM-like gene and peptidergic signaling in the last eukaryotic ...
Raj Luxmi +6 more
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Directed evolution converts subtilisin E into a functional equivalent of thermitase [PDF]
We used directed evolution to convert Bacillus subtilis subtilisin E into an enzyme functionally equivalent to its thermophilic homolog thermitase from Thermoactinomyces vulgaris.
Arnold, Frances H., Zhao, Huimin
core +2 more sources
The food enzyme subtilisin (EC 3.4.21.62) is produced with the non‐genetically modified Bacillus licheniformis strain NZYM‐CX by Novozymes A/S. The production strain met the requirements for the qualified presumption of safety (QPS) approach.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP) +25 more
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