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1 ry metabolites l-serine and 1,3-bisphospho-d-glycerate.
2 elevated urinary excretion of oxalate and L-glycerate.
3 ts for the substrates and the activator, 3-P-glycerate.
4 amic acid mutant enzyme was inhibited by 3-P-glycerate.
5 chemistry was assessed by using [14C-methyl]glycerate.
6 ereas PLGG1 alone accounts for the import of glycerate.
7 at position 382 influence the binding of 3-P-glycerate.
8 idues are not involved in the binding of 3-P-glycerate.
10 ant enzymes with apparent affinities for 3-P-glycerate 10-160-fold lower than that of the wild-type e
11 and in vivo application of sodium [1-(13)C]-glycerate ([(13)C]-Glyc) as a novel probe for evaluating
12 of yeast enolase with substrate, 2-phospho-D-glycerate (2-PGA), and product, phosphoenolpyruvate (P-e
15 midodiphosphate (Mg-AMP-PNP) and 3-phospho-D-glycerate (3-PG) has been determined by X-ray crystallog
16 starting with methyl 2,3-O-isopropylidene-d-glycerate (4) and D-ribo-phytosphingosine (3), respectiv
17 haelis constants (K(m)) for both 3-phospho-D-glycerate and ATP are increased only by three or fourfol
18 bolism as well as mineral nutrition and that glycerate and glutamine are the main metabolites respond
20 e formation of proteins and metabolites with glycerate and phosphoglycerate modifications on amino gr
21 atalyzed the NAD(+)-dependent oxidation of d-glycerate and the NADH-dependent reduction of tartronate
23 , CoMn-S spheres were synthesized using CoMn-glycerate as the precursor, followed by a sulfidation re
26 zed using an ion-exchange process to prepare glycerate-assisted CoMn-S spheres with many nanoparticle
27 , producing an operon clearly designed for d-glycerate biosynthesis from tartronate semialdehyde.
28 exchange of the alpha-proton of 2-phospho-D-glycerate but not the complete dehydration, was assayed
29 atalyzed the NAD(+)-dependent oxidation of d-glycerate but was significantly more efficient in the ox
34 achment, and intramolecular cyclization of a glycerate-derived three-carbon unit, which forms the cor
35 but forms pyruvate, rather than 3-phospho-D-glycerate, due to incapacity in protonation of the termi
36 rom inactivation most effectively, while 3-P-glycerate, fructose-1,6-P2, pyridoxal-P, and ATP plus ma
37 yed in the dehydration reaction (2-phospho-D-glycerate --> phosphoenolpyruvate + H(2)O) at different
38 (i.e. glycine not part of the production of glycerate in support of photosynthesis) is either fully
39 the progressive identification of acetyl-(R)-glycerate (k(cat)/K(m) = 4 x 10(2) M(-1) s(-1)), acetyl
40 allelic differences in 5 core genes encoding glycerate kinase (glxK), valine-pyruvate transaminase (a
41 gckA and ttuD might be structural genes for glycerate kinase and that the serine cycle and the tartr
42 gene (gckA) responsible for the activity of glycerate kinase has been identified within a chromosoma
44 dolase, tartronate semialdehyde reductase, a glycerate kinase that generates 2-phosphoglycerate as pr
45 (HCO(2)(-)) by 1,2-hydroxyl-functionalized l-glycerate (l-gly, l-HOCH(2)(HO)CHCO(2)(-)) was investiga
52 s bacterium, and instead, the bacterial-like glycerate pathway is the main route for phosphoglycolate
54 ncoding the enzymes of the d-glucarate and d-glycerate pathways (gudT, gudD, garR, garL, garK) are si
55 hat catalyzes the dehydration of 2-phospho-d-glycerate (PGA) to form phosphoenolpyruvate (PEP), is a
56 group of the substrate/product, 2-phospho-D-glycerate/phosphoenolpyruvate, and induces binding of th
61 alyzes the reduction of hydroxypyruvate to D-glycerate, the reduction of glyoxylate to glycolate and
62 then transformed through hydroxypyruvate and glycerate to enter central metabolism at phosphoglycerat
65 talyzes the conversion of hydroxypyruvate to glycerate together with the oxidation of a pyridine nucl
66 analyses, we identified Plastidal glycolate glycerate translocator 1 (PLGG1) as a candidate core pho
67 nockout line of both BASS6 and the glycolate/glycerate transporter PLGG1 (bass6, plgg1) showed an add
68 that PLGG1 is the chloroplastidic glycolate/glycerate transporter, which is required for the functio
73 uses CTP and phosphoglycerate to produce CDP-glycerate, which we hypothesize is the phosphoglycerate
74 he exchange of the C-2 proton of 2-phospho-D-glycerate with deuterium in D2O, whereas both the E211Q