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spinacia oleracea/protease
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Trienzyme treatment for food folate analysis: optimal pH and incubation time for alpha-amylase and protease treatment.
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Recent reports have indicated that trienzyme treatment before folate determination is essential to obtain the proper folate content in foods. Trienzyme treatment is performed by using alpha-amylase and protease for folate extraction from carbohydrate and protein matrices, and folate conjugase for
Identification, characterization, and molecular cloning of a homologue of the bacterial FtsH protease in chloroplasts of higher plants.
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In an attempt to identify and characterize chloroplast proteases, we performed an immunological analysis of chloroplasts using an antibody against Escherichia coli FtsH protease, which is an ATP-dependent metalloprotease bound to the cytoplasmic membrane. A cross-reacting protein of 78 kDa was found
Clp protease complexes and their diversity in chloroplasts.
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The Clp proteases represent a large, ancient ATP-dependent protease family which in higher plants is known to be located in chloroplasts. The soluble, presumably multisubunit, enzyme of the organelle stroma is of dual genetic origin. It consists of a nuclear-encoded, regulatory subunit ClpC, which
Screening for inhibitors of plant protease D1 using novel monoclonal antibodies directed against its carboxyl terminal.
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Carboxyl terminal processing protease of D1 protein (CtpA) catalyzes carboxyl terminal processing of D1 protein, which is predicted to be an excellent target for a general broad-spectrum herbicide. In this study, the CtpA gene from spinach cDNA was cloned and overexpressed and the recombinant CtpA
Overexpression and characterization of carboxyl-terminal processing protease for precursor D1 protein: regulation of enzyme-substrate interaction by molecular environments.
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CtpA, which is classified as a novel type of serine protease with a Ser/Lys catalytic dyad, is responsible for the C-terminal processing of precursor D1 protein (pD1) of the photosystem II reaction center, a process that is indispensable for the integration of water-splitting machinery in
Recognition of the structure around the site of cleavage by the carboxyl-terminal processing protease for D1 precursor protein of the photosystem II reaction center.
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In order to analyze the structural requirement(s) for proteolytic cleavage, synthetic oligopeptides corresponding to the carboxyl-terminal (COOH-terminal) sequence of the precursor to the D1 protein (pD1) of the photosystem II reaction center, with or without substituted side chain(s) around the
The 60-kDa precursor to the dithiothreitol-sensitive tetrameric protease of spinach thylakoids: structural similarities between the protease and polyphenol oxidase.
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The 60-kDa precursor to the 39-kDa dithiothreitol-sensitive protease was purified from photosystem II membranes of spinach. When partially purified 60-kDa protein was stored at 4 degrees C, the protein was degraded to fragments of 39 and 21 kDa. The 39-kDa fragment was suggested to be identical to
[Cloning, expression, purification of spinach carboxyl-terminal processing protease of D1 protein with hydrolysis activity and preparation of polyclonal antibody].
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Carboxyl-terminal processing protease of D1 protein (CtpA) catalyzes carboxyl terminal processing of the D1 protein of photosystem II, which is essential for the assembly of a manganese cluster and consequent light-mediated water oxidation. It is a target for the discovery of wide-spectrum
Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants.
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The D1 reaction center protein of the Photosystem II complex in green plants is synthesized with a short carboxyl-terminal extension. Proteolytic cleavage and removal of this extension peptide in the thylakoid lumen are necessary for the assembly of a manganese cluster that is essential for the
Spinach chloroplast ATP-dependent endopeptidase: Ti-like protease.
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The soluble fraction of spinach chloroplast was used for purification and characterization of an ATP-dependent protease. Purification included Q Sepharose Fast Flow, hydroxylapatite and FPLC Superose 6 column chromatography. The isolated enzyme requires ATP and Mg2+ for stimulation and represents a
The carboxyterminal processing protease of D1 protein: expression, purification and enzymology of the recombinant and native spinach proteins.
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The carboxyterminal processing protease of D1 protein (CtpA) is predicted to be an excellent target for a general broad-spectrum herbicide. The gene for spinach CtpA has been expressed in Escherichia coli. The expressed protein that was found mainly in inclusion bodies has been purified and refolded
Evidence for a novel ATP-dependent membrane-associated protease in spinach leaf mitochondria.
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We report the presence of an ATP-dependent proteolytic activity in spinach (Spinacia oleracea) leaf mitochondria. The proteolysis was observed as degradation of newly imported precursor protein. The precursor studied was that of the ATP synthase F1 beta subunit of Nicotiana plumbaginifolia,
Biochemical and molecular characterization of senescence-related cysteine protease-cystatin complex from spinach leaf.
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Cysteine proteases (CPs) with N-succinyl-Leu-Tyr-4-methylcoumaryl-7-amide (Suc-LY-MCA) cleavage activity were investigated in green and senescent leaves of spinach. The enzyme activity was separated into two major and several faint minor peaks by hydrophobic chromatography. These peaks were
Carboxyl-terminal processing protease for the D1 precursor protein: cloning and sequencing of the spinach cDNA.
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A previous study has demonstrated that the carboxyl-terminal (C-terminal) processing protease in spinach for the D1 precursor protein (pDl) of the photosystem II reaction center is a monomeric protein of about 45 kDa. Based on the amino acid sequence data of the purified protease, a cDNA clone
Light-induced D1 protein degradation is catalyzed by a serine-type protease.
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Light-induced degradation of the D1 protein in isolated spinach photosystem II core preparations was studied after addition of various protease inhibitors. The degradation was selectively inhibited by several serine protease inhibitors in particular diisopropylfluorophosphate. The results
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