ライフサイエンスコーパス: acetylmuramic acid

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1 peptidoglycan (PG) at the C-6 position on N-acetylmuramic acid.

2 ccurrence of N-glycolylmuramic rather than N-acetylmuramic acid.

3 -links by cleaving the peptide moiety from N-acetylmuramic acid.

4 roup to activate the carboxyl group of UDP-N-acetylmuramic acid.

5 ciate with the repeating disaccharide beta-N-acetylmuramic acid, (1-->4)-beta-N-acetylglucosamine of

6 The N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) u

7 Peptidoglycan is made of repeating N-acetylmuramic acid and N-acetylglucosamine disaccharides

8 ating disaccharide unit of beta-1,4-linked N-acetylmuramic acid and N-acetylglucosamine.

9 oglycan; group B carbohydrate is linked to N-acetylmuramic acid, and capsular polysaccharide is linke

10 Here we show that the 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) is returned to the biosyn

11 med AmiD, as a possible second 1,6-anhydro-N-acetylmuramic acid (anhMurNAc)-l-alanine amidase in Esch

12 066 and SL1067 were required for growth on N-acetylmuramic acid as a sole carbon source.

13 formed by linear glycan chains composed of N-acetylmuramic acid-(beta-1,4)-N-acetylglucosamine (MurNA

14 s also retain more diaminopimelic acid and N-acetylmuramic acid during germination than wild-type spo

15 se of naked glycans containing 1,6-anhydro N-acetylmuramic acid ends.

16 ide, N-acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-anhMurNAc).

17 The M. smegmatis mutant is devoid of UDP-N-acetylmuramic acid hydroxylase activity and synthesizes

18 e gene namH encoding the mycobacterial UDP-N-acetylmuramic acid hydroxylase by computer data base sea

19 ed a novel assay for the mycobacterial UDP-N-acetylmuramic acid hydroxylation reaction and demonstrat

20 nd between N-acetylglucosamine and anhydro-N-acetylmuramic acid in cell wall degradation products fol

21 by acetylation of the C6 hydroxyl group of N-acetylmuramic acid in the PG glycan backbone.

22 al C3 enolpyruvyl substrate, to UDP-methyl-N-acetylmuramic acid in the presence of NADPH.

23 peptidoglycan recycling enzyme 1,6-anhydro-N-acetylmuramic acid kinase (AnmK) from Pseudomonas aerugi

24 on to the structurally related 1,6-anhydro-N-acetylmuramic acid kinase (AnmK), it forms markedly fewe

25 e sugar is first phosphorylated by anhydro-N-acetylmuramic acid kinase (AnmK), yielding MurNAc-P, and

26 determinant of the pneumococcal autolysin (N-acetylmuramic acid-L-alanine amidase).

27 UDP-N-acetylmuramic acid:L-alanine ligase (MurC) catalyzes the

28 hermore, E. coli also recycles the anhydro-N-acetylmuramic acid moiety by first converting it into N-

29 s the beta-1,4 glycosidic linkages between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (Glc

30 polymer, consisting of a linear, repeating N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (Glc

31 ternating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) units, cross-linked via pept

32 units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc), which are cross-linked by s

33 nscription by binding the PG precursor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide.

34 The muramyl residue is present as N-acetylmuramic acid, N-glycolylmuramic acid, and muramic

35 ase of SpA by removing amino sugars [i.e., N-acetylmuramic acid-N-acetylglucosamine (MurNAc-GlcNAc)]

36 s the cleavage of glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine residue

37 alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) cross-linked by short peptide s

38 ing units of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) with an appended peptide.

39 e repeats of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM).

40 up of un-cross-linked peptides attached to N-acetylmuramic acid partially substituting the function o

41 on the detection of the cell precursor UDP-N-acetylmuramic acid pentapeptide intermediate terminating

42 empedopeptin is undecaprenyl pyrophosphate-N-acetylmuramic acid(pentapeptide)-N-acetylglucosamine (li

43 of the soluble peptidoglycan precursor UDP-N-acetylmuramic acid-pentapeptide (UDP-MurNAc-pentapeptide

44 of the murein precursor, Lipid I, from UDP-N-acetylmuramic acid-pentapeptide and the lipid carrier, u

45 timate soluble peptidoglycan precursor UDP-N-acetylmuramic acid-pentapeptide in the cytoplasm.

46 MurQ is an N-acetylmuramic acid-phosphate (MurNAc-P) etherase that co

47 onversion of the 2,3-dideuterio-UDP-methyl-N-acetylmuramic acid product to 2,3-dideuterio-2-hydroxybu

48 s removal of a peptide side chain from the N-acetylmuramic acid residue by a cwlD-encoded muramoyl-L-

49 ions of Asn46 and Asp52 with the D-subsite N-acetylmuramic acid residue help to distort that pyranose

50 ees of polymerization and terminating with N-acetylmuramic acid residues at the reducing ends.

51 he deep end of a long binding groove, with N-acetylmuramic acid situated in the middle of the groove,

52 nd human clinical strains, did not require N-acetylmuramic acid supplementation for growth as pure cu

53 e dehydrogenase operon, genes required for N-acetylmuramic acid synthesis, a 14-gene gas vesicle clus

54 peptide is amide-linked to the carboxyl of N-acetylmuramic acid, thereby tethering the COOH-terminal

55 as an enzyme activity that can convert UDP-N-acetylmuramic acid to UDP-N-glycolylmuramic acid.

56 samine deacetylase (Pgd) and acetylated by O-acetylmuramic acid transferase (Oat).

57 residues are ligated to uridine diphospho-N-acetylmuramic acid (UDP-MurNAc).

58 zae MurC in complex with its substrate UDP-N-acetylmuramic acid (UNAM) and Mg(2+) and of a fully asse

59 e of a 40-fold excess of uridine diphospho N-acetylmuramic acid (UNAM) either aerobically or anaerobi

60 endent ligation of L-alanine (Ala) and UDP-N-acetylmuramic acid (UNAM) to form UDP-N-acetylmuramyl-L-

61 xists in a tightly locked complex with UDP-N-acetylmuramic acid (UNAM), the product of the MurB react

62 Modification of N-acetylmuramic acid with wall teichoic acid, a ribitol-ph

63 ide units (N-acetylglucosamine-[beta-1, 4]-N-acetylmuramic acid) with different degrees of polymeriza

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