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1 ng the gamma carboxylate of the substrate in glutamate mutase.
2 ognizing the amino group of the substrate in glutamate mutase.
3 ate and product in the reaction catalyzed by glutamate mutase.
4 to constructed for the reaction catalyzed by glutamate mutase.
5 pectrum is also observed for AdoCbl bound to glutamate mutase.
6 w similar mutations in the "DXHXXG" motif of glutamate mutase affect coenzyme binding and catalysis i
7 e ligands in the cobalamin-dependent enzymes glutamate mutase and methionine synthase.
8                This reaction is catalyzed by glutamate mutase, but k(cat) = 0.05 s(-)(1) is much lowe
9                  Adenosylcobalamin-dependent glutamate mutase catalyzes an unusual carbon skeleton re
10                                              Glutamate mutase catalyzes the reversible isomerization
11  that expected from the crystal structure of glutamate mutase complexed with the substrate.
12 icant degree of hydrogen tunneling occurs in glutamate mutase, even though the intrinsic kinetic isot
13                                              Glutamate mutase (GM) is a cobalamin-dependent enzyme th
14 ost-homolysis product Co2+ Cbl when bound to glutamate mutase in the presence of substrate (or a subs
15           Binding of 2-methyleneglutarate to glutamate mutase initiates homolysis of adenosylcobalami
16                                              Glutamate mutase is comprised of two weakly associating
17                                              Glutamate mutase is one of a group of adenosylcobalamin-
18                                              Glutamate mutase is one of a group of adenosylcobalamin-
19                                              Glutamate mutase is one of a group of adenosylcobalamin-
20                                              Glutamate mutase is one of several adenosylcobalamin-dep
21 that occurs when adenosylcobalamin-dependent glutamate mutase is reacted with the substrate analogue
22 ope effects associated with this process for glutamate mutase reacting with deuterated glutamate.
23 osition of the catalytic domains of ThiC and glutamate mutase shows that these two enzymes share simi
24  2-methyleneglutarate mutase, it reacts with glutamate mutase to cause time-dependent inhibition of t
25 with the formation of 5'-deoxyadenosine when glutamate mutase was reacted with [5'-(3)H]adenosylcobal
26                    For one of these enzymes, glutamate mutase, we have investigated whether hydrogen
27    The mutations made in the MutS subunit of glutamate mutase were His16Gly, His16Gln, Asp14Asn, Asp1
28         We have investigated the reaction of glutamate mutase with the glutamate analogue, 2-thiolglu
29             Here we describe the reaction of glutamate mutase with the substrate analog, 2-ketoglutar

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