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1 s yet is widely required by eukaryotes as an enzyme cofactor.
2 centrations and converts 5-formylTHF into an enzyme cofactor.
3 6), plays a pivotal role in metabolism as an enzyme cofactor.
4 ace if the ultramicroelectrode generates the enzyme cofactor.
5 tion of modulators of enzyme activity and of enzyme cofactors.
6 tracellular iron to synthesize steroidogenic enzyme cofactors.
7 s of several cellular metabolites, including enzyme cofactors.
11 .org) has implemented a pipeline to identify enzyme cofactor and cofactor-like molecules, which are n
12 enine dinucleotide (NAD(+)) is an endogenous enzyme cofactor and cosubstrate that has effects on dive
13 tical micronutrient for cells, serving as an enzyme cofactor and protecting against oxidative stress.
19 cob(III)alamin is the probable physiological enzyme cofactor, and cob(II)alamin rather than cob(I)ala
25 that in addition to its catalytic role as an enzyme cofactor, biotin has multiple roles in regulating
26 itamin supplementation supports the need for enzyme cofactors but cannot provide substrate in the for
28 peptide bond to the catalytic cleft of this enzyme-cofactor complex does not significantly contribut
29 el we conclude that the resting state of the enzyme-cofactor complex is such that the cofactor is alr
30 at the pool of exchangeable hydrogens in the enzyme-cofactor complex is two-a finding consistent with
31 th previous NMR studies of the apoenzyme and enzyme-cofactor complex provide snapshots of the pathway
32 rolytic activity of the resulting artificial enzyme-cofactor complex was tuned by the number and dept
37 signed ternary complex, data for the binary (enzyme-cofactor) complex were collected, providing chemi
39 molecular substrate docking with coagulation enzyme-cofactor complexes involves multiple contacts dis
40 serine proteases that typically function in enzyme-cofactor complexes, exemplified by coagulation fa
41 ssociated with the stable confinement of the enzyme/cofactor couple (HBD/NAD(+)) and with a stable an
43 chemical activity was investigated using the enzyme cofactor dihydronicotinamide adenine dinucleotide
45 the amounts of tetrahydrobiopterin (BH4), an enzyme cofactor essential for the synthesis of several n
46 es a reaction in two parts: reduction of the enzyme cofactor FAD by NADPH in response to binding p-hy
48 es a reaction in two parts: reduction of the enzyme cofactor, FAD, by NADPH in response to binding p-
49 voltammetric peaks were due to the redox of enzyme cofactor flavin adenine dinucleotide (FAD), which
50 le structure and function via its role as an enzyme cofactor for collagen and carnitine biosynthesis.
51 rofolate, is replenished and available as an enzyme cofactor for numerous cellular reactions, includi
53 form of vitamin B12 that is best known as an enzyme cofactor, has expanded the number of known photor
58 ata extracted from the literature on organic enzyme cofactors in biocatalysis, as well as automatical
60 urface amino acid residues, so understanding enzyme-cofactor interactions is important for the design
62 m to better understand the way in which this enzyme cofactor is built and the role of these metalloen
64 tigated metabolic precursor to the prominent enzyme cofactor NAD(+), where it is assumed that deliver
68 rial, of novel, bioactive derivatives of the enzyme cofactor nicotinamide adenine dinucleotide (NAD).
70 ements lanthanides (Ln(3+) ) have emerged as enzyme cofactors of methanol dehydrogenases of the XoxF
71 tinamide adenine dinucleotide (NAD(+)) is an enzyme cofactor or cosubstrate in many essential biologi
76 methodology for the generation of orthogonal enzyme/cofactor pairs promises to expand cofactor divers
79 Thiamin pyrophosphate (TPP) is an essential enzyme cofactor required for the viability of all organi
82 nucleosome complex and only compete with the enzyme cofactor SAM (S-adenosyl-L-methionine) but not th
83 availability of desired cofactor, changes in enzyme cofactor specificity, and introduction of novel r
85 oach to probe the conformational changes and enzyme/cofactor/substrate interactions that contribute t
86 siae to account for proteome constraints and enzyme cofactors such as metal ions, named CofactorYeast
90 class of nutrients, cobamides (the family of enzyme cofactors that includes vitamin B(12)), is widely
93 nal repurposing of adenosylcobalamin from an enzyme cofactor to a light sensor, we find that nature a
97 hate (PLP) is a fundamental, multifunctional enzyme cofactor used to catalyze a wide variety of chemi
98 of proteins bound to common metabolites and enzyme cofactors, we identify a large set of mostly unex