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1 edition of Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors found in the catalog.

Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors

Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors

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  • 26 Currently reading

Published by Plenum Press in New York .
Written in English

    Subjects:
  • Phospholipase A2 -- Congresses.,
  • Phospholipase A2 -- Mechanism of action -- Congresses.,
  • Phospholipase A2 -- Inhibitors -- Congresses.,
  • Phospholipases -- antagonists & inhibitors -- congresses.,
  • Phospholipases -- physiology -- congresses.

  • Edition Notes

    Statementedited by Anil B. Mukherjee.
    SeriesAdvances in experimental medicine and biology ;, v. 279
    ContributionsMukherjee, Anil B.
    Classifications
    LC ClassificationsQP609.P553 B56 1990
    The Physical Object
    Paginationviii, 264 p. :
    Number of Pages264
    ID Numbers
    Open LibraryOL1860870M
    LC Control Number90014266

      Phospholipase C catalyze the hydrolysis of Phosphatidyl inositol 4,5 biphosphate that is forming part of the plasma membrane. The action of the enzyme on this substrate produces IP3 (Inositol triphosphate) and diacylglycerol. IP3 difuses into the cytosol and binds to its receptor in the sarcoplasmic reticulum and opens a Calcium channel. The effector proteins activated (or inactivated) by trimeric G proteins are either enzymes that form second messengers (e.g., adenylyl cyclase, phospholipase C) or ion channels (see Table ). In each case, it is the Gαsubunit that determines the function of the G protein and affords its specificity.

      Plant phospholipase A: advances in molecular biology, biochemistry, and cellular function Plant phospholipase A: advances in molecular biology, biochemistry, and cellular function Chen, Guanqun; Greer, Michael S.; Weselake, Randall J. Abstract Plant phospholipase As (PLAs) are a complex group of enzymes that catalyze the release of free fatty acids from phospholipids. Bovine pancreatic phospholipase A2 (PLA2), a small ( kDa) Ca2+-dependent lipolytic enzyme, is rich in functional and structural character. In an effort to examine its detailed structure−function relationship, we determined its solution structure by multidimensional nuclear magnetic resonance (NMR) spectroscopy at a functionally relevant by:

    Molecular Biology of the Cell Vol. 21, No. 23 Articles Free Access ADP Ribosylation Factors 1 and 4 and Group VIA Phospholipase A 2 Regulate Morphology and Intraorganellar Traffic in the Endoplasmic Reticulum–Golgi Intermediate Compartment. Binding Conformation of 2-Oxoamide Inhibitors to Group IVA Cytosolic Phospholipase A2 Determined by Molecular Docking Combined with Molecular Dynamics. Journal of Chemical Information and Modeling , 52 (1), Cited by:


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Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors Download PDF EPUB FB2

Get this from a library. Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors.

[Anil B Mukherjee;] -- Proceedings of a symposium in Bethesda, Maryland, Septemberwhich focused on the enzyme phospholipase A2, associated with cellular signal transduction, and the generation of many cellular.

"Proceedings of a symposium on Biochemistry, molecular biology, and physiology of phospholipase A₂ and its regulatory factors, held Sept.in Bethesda, Maryland"--Title page verso.

Description: 1 online resource (viii, pages): illustrations (some color) Molecular biology Phospholipases, Enzymes That Share a Substrate Class This symposium was organized to obtain an overview of current investigations on this enzyme from the standpoint of its chemistry, molecular biology and physiology.

Another important focus of this symposium concerns the regulation of PLA2, including endogenous and. Phospholipase D (PLD) also is a phosphodiesterase that catalyzes hydrolysis of a head group, leaving phosphatidate.

molecular biology A phospholipase B, capable of hydrolyzing the carboxylic ester at the sn-1 or sn-2 position has been postulated, however, this is probably another enzyme with the preferred name lysophospholipase.

In Laboratory Techniques in Biochemistry and Molecular Biology, Substrate specificity. The specificity for phospholipid classes of the EDTA-insensitive PLA 1 of rat brain was determined by deacylation of [3 H]glycerol-labeled PtdIns, PtdEtn and PtdCho and measuring the formation of corresponding lysophospholipids (Ueda et al.

Hirata F., Hirata A. () Biology of Phospholipase Inhibitory Proteins. In: Mukherjee A.B. (eds) Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors.

Advances in Experimental Medicine and Biology, vol Cited by: 7. Plant phospholipase A: advances in molecular biology, biochemistry, and cellular function. Chen G, Greer MS, Weselake RJ. Plant phospholipase As (PLAs) are a complex group of enzymes that catalyze the release of free fatty acids from phospholipids.

Plant PLAs can be grouped into three families, PLA1, PLA2, and patatin-like PLA, that catalyze Cited by: The phospholipase A 2 (PLA 2) superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different products of this reaction, a free fatty acid, and lysophospholipid have many different important physiological roles.

There are five main types of PLA 2: the secreted sPLA 2 ’s, the cytosolic cPLA 2 ’s, the Ca Cited by: Buy The Phospholipase C Pathway: Its Regulation and Desensitization (Molecular Biology Intelligence Unit) on FREE SHIPPING on qualified orders.

Plant Phospholipase A: Advances in molecular biology, biochemistry and cellular function Article Literature Review in Biomolecular concepts July with 58 Reads How we measure 'reads'.

Potential factors involved in host growth include three copies of phospholipase A2, an enzyme that is rare in bacteria but implicated in a range of plant cellular processes, and proteins. Phospholipase A2 (PLA2) designates a class of enzymes that hydrolyze the sn-2 ester of glycerophospholipids to produce a fatty acid and a lysophospholipid.

It has become clear that some of these enzymes liberate arachidonic acid in mammalian cells for the biosynthesis of eicosanoids, and thus there has been considerable interest in developing PLA2 inhibitors. Phospholipase A2 in Clinical Inflammation presents an up-to-date topical review of the biochemistry, molecular biology, and biology of mammalian phospholipase A2 (PLA2).

The emphasis of this monograph is on the current aspects of PLA2 research using molecular approaches to investigate PLA2 structure and function, inhibitor design, and the. Regulation and physiological functions of mammalian phospholipase C Yoshikazu Nakamura Regulation and physiological functions of mammalian phospholipase C, The Journal of Biochemistry, VolumeIssue 4, AprilThe molecular heterogeneity of protein kinase C and its implications for cellular by: Phospholipase Cβ (PLCβ) enzymes hydrolyze phosphatidylinositol 4,5-bisphosphate to produce second messengers that regulate intracellular Ca 2+, cell proliferation, and activity is dependent upon interfacial activation that occurs upon localization to cell membranes.

Phospholipase C (PLC) is a class of membrane-associated enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which play an important role in eukaryotic cell physiology, in particular signal transduction pathways.

There are thirteen kinds of mammalian phospholipase C that are classified. cytes. The activator induced phospholipase D (PLD) ac-tivity, and its effect on the release of the TG-containing structures from the microsomes was inhibited by 1-buta-nol (but not 2-butanol) or 2,3-diphosphoglycerate.

The ac-tivator could be replaced by a constitutively active PLD or phosphatidic acid. These results indicate that PLD and. Phospholipases A2 (PLA2s) EC are enzymes that cleave fatty acid in position two of phospholipids, hydrolyzing the bond between the second fatty acid “tail” and the glycerol molecule.

This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond, releasing arachidonic acid and lysophosphatidic : BRENDA entry.

Molecular Biology of the Cell Vol. 16, No. 9 Articles Free Access Na/K-ATPase Tethers Phospholipase C and IP3 Receptor into a Calcium-regulatory Complex This is the final version - click for previous version.

How cells regulate G q efficacy (initiation and termination of G q signaling) to effect response remains a central question in pharmacology and drug discovery. Phospholipase C‐β 1 (PLC‐β 1) is an effector and a GTPase activating protein (GAP) specific to Gα physiological function of PLC‐β 1 GAP remains unclear and controversial.

GAPs are generally thought to function in Cited by: 1. USA Home > Product Directory > Biochemicals and Reagents > Enzymes, Inhibitors, and Substrates > Enzyme Substrates > Substrates by Enzyme > Phospholipase A2 .This review focuses on two phospholipase activities involved in eukaryotic signal transduction.

The action of the phosphatidylinositol-specific phospholipase C enzymes produces two well-characterized second messengers, inositol 1,4,5-trisphosphate and diacylglycerol. This discussion emphasizes recent advances in elucidation of the mechanisms of regulation and catalysis of the various isoforms Cited by:   Phospholipases are a complex group of enzymes that hydrolyze phospholipids.

The plant phospholipase family is composed of multiple members with varying positional specificity, and each type is represented by multiple isoforms distinguishable by their structural, catalytic, and physiological characteristics. A large number of phospholipase genes and gene families have been identified and Cited by: