5 edition of Signal peptidases found in the catalog.
Includes bibliographical references and index.
|Statement||[edited by] Gunnar von Heijne.|
|Series||Molecular biology intelligence unit, Molecular biology intelligence unit (Unnumbered)|
|Contributions||Heijne, Gunnar von.|
|LC Classifications||QP609.S53 H45 1994|
|The Physical Object|
|Pagination||xi, 127 p. :|
|Number of Pages||127|
|LC Control Number||94037493|
Signal Peptidases. Signalna peptidaza I (EC , vodeća peptidaza I, signalna proteinaza, Escherichia coli vodeća peptidaza, eukariotska signalna peptidaza, eukariotska signalna proteinaza, vodeća peptidaza, vodeća peptidna hidrolaza, vodeća proteinaza, signalna peptidaza, pilinska vodeća peptidaza, SPC, prokariotska signalna peptidaza, prokariotska vodeća peptidaza, HOSP, prokariotska signalna BRENDA: BRENDA entry.
Plant plastids and mitochondria have dynamic proteomes. Protein homeostasis in these organelles is maintained by a proteostasis network containing protein chaperones, peptidases, and their substrate recognition factors. However, many peptidases, as well as their functional connections and substrates, are poorly characterized. This review provides a systematic insight into the organellar Cited by: 7. Define peptidase. peptidase synonyms, peptidase pronunciation, peptidase translation, English dictionary definition of peptidase. Related to peptidase: signal peptidase. peptidase KEY WORDS: Homarus americanus, aspartic peptidase, cysteine peptidases, crustacean protein digestion, American lobster. Bacterial type I signal peptidases (SPases) are membrane-anchored serine proteases that process the signal peptides of proteins exported via the Sec and Tat secretion systems. Despite their crucial importance for bacterial virulence and their attractiveness as drug targets, only one such enzyme, LepB from Escherichia coli, has been structurally characterized, and the transient nature of Cited by: 7.
In molecular biology, the Signal Peptide Peptidase (SPP) is a type of protein that specifically cleaves parts of other proteins. It is an intramembrane aspartyl protease with the conserved active site motifs 'YD' and 'GxGD' in adjacent transmembrane domains (TMDs). Its sequences is highly conserved in different vertebrate species. SPP cleaves remnant signal peptides left behind in membrane by InterPro: IPR Thylakoids are the chloroplast internal membrane systems that house light-harvesting and electron transport reactions. Despite the important functions and well-studied constituents of thylakoids, the molecular mechanism of their development remains largely elusive. A recent genetic study has demonstrated that plastidic type I signal peptidase 1 (Plsp1) is vital for proper thylakoid development Cited by: The Signal Peptide Peptidases (SPP) are members of the Intramembrane Cleaving Proteases, which are involved in an array of protein-processing and intracellular signaling events in animals. Arabidopsis (Arabidopsis thaliana) has six genes encoding SPP-like proteins, the physiological functions of which are unknown. As a first step in defining the roles of the SPPs in plants, we Cited by:
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SyntaxTextGen not activatedUpon passage through the ER, the pdf peptide is cleaved by signal peptidases. Signal peptidases are highly sequence‐specific enzymes and efficiently remove the signal peptides that are.
A novel bacterial target presented in the book Proteases of Download pdf Agents, is the type I signal peptidase. This protease is pivotal to the exportation of proteins from the cytoplasm since removal of the signal peptide is required for proper release of the secreted protein as well as for proper localization of membrane proteins with cleaved Cited by: 3.NEW (August ): A book chapter on SignalP ebook been published: Predicting Secretory Proteins with SignalP Henrik Nielsen In Kihara, D (ed): Protein Function Prediction (Methods in Molecular Biology vol.
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