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Literature summary for 1.2.1.13 extracted from

  • Negi, S.S.; Carol, A.A.; Pandya, S.; Braun, W.; Anderson, L.E.
    Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts (2008), J. Struct. Biol., 161, 18-30.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular docking of ferredoxin-NADP-reductase EC 1.18.1.2 and GAPD. enzymes are able to form at least two different complexes, one involving a single GAPD monomer and an ferredoxin-NADP-reductase monomer or dimer. The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer or dimer. Ferredoxin is able to interact with FNR in either complex Spinacia oleracea

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast GAPD is colocalized with ferredoxin-NAPD reductase in chloroplasts Pisum sativum 9507
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chloroplast ferredoxin-NADP-reductase EC 1.18.1.2 and GAPD are co-localized, suggesting that ferredoxin-NADP-reductase might carry FADH2 or NADPH from the thylakoid membrane to GAPD, or that ferredoxin might carry electrons to ferredoxin-NADP-reductase Pisum sativum 9507
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Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-
Pisum sativum
-
variant Little Marvel
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Spinacia oleracea P19866
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Pisum sativum
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leaf
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Spinacia oleracea
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
Pisum sativum 3-phospho-D-glyceroyl phosphate + NADPH + H+
-
?

Synonyms

Synonyms Comment Organism
GAPD
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Pisum sativum
NAPD-linked glyceraldehyde-3-P dehydrogenase
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Pisum sativum

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Pisum sativum