Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

Reference on EC 1.1.1.82 - malate dehydrogenase (NADP+) and Organism(s) Sorghum bicolor and UniProt Accession P17606

Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luchetta, P.; Cretin, C.; Gadal, P.
Structure and characterization of the Sorghum vulgare gene encoding NADP-malate dehydrogenase
Gene
89
171-177
1990
Sorghum bicolor
Manually annotated by BRENDA team
Krimm, I.; Goyer, A.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Lancelin, J.M.
Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition
J. Biol. Chem.
274
34539-34542
1999
Sorghum bicolor
Manually annotated by BRENDA team
Cretin, C.; Luchetta, P.; Joly, C.; Decottignies, P.; Lepiniec, L.; Gadal, P.; Sallantin, M.; Huet, J.C.; Pernollet, J.C.
Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)
Eur. J. Biochem.
192
299-303
1990
Sorghum bicolor
Manually annotated by BRENDA team
Johansson, K.; Ramaswamy, S.; Saarinen, M.; Lemaire-Chamley, M.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Eklund, H.
Structural basis for light activation of a chloroplast enzyme: The structure of Sorghum NADP-malate dehydrogenase in its oxidized form
Biochemistry
38
4319-4326
1999
Sorghum bicolor (P17606)
Manually annotated by BRENDA team
Hirasawa, M.; Ruelland, E.; Schepens, I.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Knaff, D.B.
Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase
Biochemistry
39
3344-3350
2000
Sorghum bicolor, Sorghum sp.
Manually annotated by BRENDA team
Jacquot, J.P.; Keryer, E.; Issakidis, E.; Decottignies, P.; Miginiac-Maslow, M.; Schmitter, J.M.; Cretin, C.
Properties of recombinant NADP-malate dehydrogenases from Sorghum vulgare leaves expressed in Escherichia coli cells
Eur. J. Biochem.
199
47-51
1991
Sorghum bicolor
Manually annotated by BRENDA team
Rondeau, P.; Rouch, C.; Besnard, G.
NADP-malate dehydrogenase gene evolution in Andropogoneae (Poaceae): gene duplication followed by sub-functionalization
Ann. Bot.
96
1307-1314
2005
Chrysopogon zizanioides (Q8H0J7), Chrysopogon zizanioides (Q8L5S9), Dichanthium aristatum (Q8H0R5), Flaveria trinervia (Q42737), Heteropogon contortus (Q2MG92), Hyparrhenia rufa (Q2MG94), Ischaemum koleostachys (Q8H0Q3), Megathyrsus maximus (Q8H0N9), Melinis repens (Q2MG93), Oplismenus compositus (Q8H0P4), Oryza sativa, Paspalum paniculatum (Q8H0N5), Pogonatherum paniceum (Q8H0N4), Saccharum hybrid cultivar R570 (Q4W4C2), Saccharum officinarum (Q1RS10), Saccharum officinarum (Q8L6C8), Saccharum spontaneum (Q8H0M0), Setaria geminata (Q1RS11), Sorghum arundinaceum (Q8H0L7), Sorghum bicolor (P17606), Sorghum bicolor (P37229), Themeda quadrivalvis (Q8H0K0), Zea mays (P15719)
Manually annotated by BRENDA team