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NADP-dependent enzymes and abiotic stress

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10127301" target="_blank" >RIV/00216208:11310/12:10127301 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    NADP-dependent enzymes and abiotic stress

  • Original language description

    Abiotic stress often negatively affects photosynthesis, which is the main source of NADPH. Reduced form of the coenzyme represents an indispensable compound for biosynthetic reactions, antioxidant systems, and for enzymes involved in regulation. As the ratio NADP+/NADPH in plants influences redox reactions, the control of cell redox homeostasis is important for balancing metabolic processes and redox-dependent signalling. NADPH is produced mainly by enzymes from oxidative pentose phosphate pathway (glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase) but also other enzymes (e.g. NADP-isocitrate dehydrogenase, NADP-malic enzyme, NADP-glutamate dehydrogenase, and non-phosphorylating NADP-glyceraldehyde-3-phosphate dehydrogenase) representan alternative source of NADPH in stressed plants. NADP-glutamate dehydrogenase is involved in catabolism of proteins and amino acids and thus provides NADPH. However, the role of this enzyme could be different under stress condition (e.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Book/collection name

    Abiotic Stress: New Research

  • ISBN

    978-1-61942-197-4

  • Number of pages of the result

    42

  • Pages from-to

    57-98

  • Number of pages of the book

    201

  • Publisher name

    Nova Science Publischers

  • Place of publication

    Hauppauge, N.Y., USA

  • UT code for WoS chapter