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1 rolysis of N-acyl-substituted derivatives of d-glutamate.
2 was found that these fusion proteins retain D-glutamate-adding activity and have Km and Vmax values
4 dered solely responsible for biosynthesis of D-glutamate, an essential component of cell wall peptido
5 acterial enzyme that converts l-glutamate to d-glutamate, an essential precursor for peptidoglycan sy
7 sired E-olefin isosteres of L-glutamyl-gamma-D-glutamate and L-glutamyl-gamma-L-glutamate, following
8 shown that both isoforms cocrystallize with d-glutamate as dimers, and the enzyme is in a closed con
9 eted CapD, an enzyme that cleaves poly-gamma-D-glutamate capsule and generates amide bonds with pepti
10 nd the primary constituent of the poly-gamma-d-glutamate capsule of the pathogen Bacillus anthracis.
11 ha, is significantly different than the RacE-D-glutamate complex on the basis of the crystal structur
13 ved only in minimal medium supplemented with D-glutamate, demonstrating that MurI is essential for gr
14 -like protein (ChiW) and a putative l-alanyl-d-glutamate endopeptidase (ChiX), and subsequent biochem
15 yme involved in the stereoinversion of L- to D-glutamate for peptidoglycan biosynthesis, glutamate ra
16 hat glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in M. smegmatis.
17 e relative quantification of d-aspartate and d-glutamate in individual neurons mechanically isolated
18 , because L-glutamate stereoisomerization to D-glutamate is predicted to be closely associated with p
19 = 5.2 x 10(6) M(-1) s(-1)), and l-methionine-d-glutamate (k(cat)/K(m) = 3.4 x 10(5) M(-1) s(-1)).
20 t)/K(m) = 5.8 x 10(6) M(-1) s(-1)), N-acetyl-d-glutamate (k(cat)/K(m) = 5.2 x 10(6) M(-1) s(-1)), and
21 best substrates for this enzyme are N-formyl-d-glutamate (k(cat)/K(m) = 5.8 x 10(6) M(-1) s(-1)), N-a
22 synthase (GshA), UDP-N-acetylmuramoylalanine-D-glutamate ligase (MurD) and glutamate racemase (MurI).
24 are predominantly N-acetylmuramyl-L-alanine-D-glutamate-meso-diaminopimelic acid-D-alanyl-D-alanine,
25 us aureus MurE UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase (MurE) (E.C.
26 main resembles UDP-N-acetylmuramoyl-L-alanyl-D-glutamate:meso-diaminopimelate ligase (MurE), yet the
28 a unique polyglutamic acid polymer in which D-glutamate monomers are joined by gamma-peptidyl bonds.
30 ccine by conjugating the capsular poly-gamma-d-glutamate (PGA) with PA to elicit the production of an
31 n used as a target for drug development, and d-glutamate, synthesized by glutamate racemase (MurI), i
32 yme, catalyzes the ATP-dependent addition of D-glutamate to an alanyl residue of the UDP-N-acetylmura
34 and RacE2 to catalyze the rapid formation of d-glutamate, we have determined that RacE1 and RacE2 are
35 . anthracis RacE1 and RacE2, in complex with d-glutamate, were determined to resolutions of 1.75 A an
36 is responsible for converting l-glutamate to d-glutamate, which is an essential component of peptidog
37 sible stereoisomerization of L-glutamate and D-glutamate with similar, but not identical, steady-stat
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