umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
KINETICS AND REGULATION OF THE NAD(P)H-DEPENDENT GLYOXYLATE-SPECIFIC REDUCTASE FROM SPINACH LEAVES
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC). (Leszek Kleczkowski)ORCID iD: 0000-0001-8685-9665
1995 (English)In: Zeitschrift für Naturforschung C - A Journal of Biosciences, ISSN 0939-5075, E-ISSN 1865-7125, Vol. 50, no 1-2, 21-28 p.Article in journal (Refereed) Published
Abstract [en]

Kinetic mechanism of purified spinach leaf NAD(P)H glyoxylate reductase (GR-1) was studied using either NADPH and NADH as alternative substrates with glyoxylate. The mechanism was elucidated from substrate kinetic patterns using NADH as a cofactor rather than NADPH. With NADPH varied versus glyoxylate, and with NADPH and glyoxylate varied at a constant ratio, the patterns obtained on double reciprocal plots appeared to be consistent with a ping-pong mechanism; however, kinetic patterns with NADH conclusively ruled out the ping-pong reaction in favour of the sequential addition of the reactants. Product inhibition studies with glycolate and NADP have suggested either that NADPH binds to the enzyme before glyoxylate or that the addition of substrates is a random one. Studies with active group modifiers suggested an involvement of histidine, serine and cysteine residues in GR-1 activity. Salts had little or no effect on the activity of the enzyme, with the exception of cyanide, which had an apparent K-i of ca. 2 mM. Studies with several metabolites used as possible effecters of GR-1 activity have suggested that the enzyme is modulated only by substrate availability in vivo. The apparent insensitivity of GR-1 to metabolic effecters is consistent with the proposed role of the enzyme in detoxifying glyoxylate which may act as a potent inhibitor of photosynthetic processes in plant tissues.

Place, publisher, year, edition, pages
1995. Vol. 50, no 1-2, 21-28 p.
Keyword [en]
ALTERNATIVE SUBSTRATE, CYANIDE, CYTOSOL, GLYCOLATE PATHWAY, GLYOXYLATE REDUCTASE
Identifiers
URN: urn:nbn:se:umu:diva-44754ISI: A1995QK48000004OAI: oai:DiVA.org:umu-44754DiVA: diva2:424376
Available from: 2011-06-17 Created: 2011-06-09 Last updated: 2017-12-11

Open Access in DiVA

No full text

Authority records BETA

Kleczkowski, Leszek A

Search in DiVA

By author/editor
Kleczkowski, Leszek A
By organisation
Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)
In the same journal
Zeitschrift für Naturforschung C - A Journal of Biosciences

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 21 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf