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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

The d-glutamate-adding and d-alanyl-d-alanine-adding enzymes from Escherichia coli were partially purified by fast protein liquid chromatography on an anion exchanger. Their relative molecular masses, determined by gel filtration on Superose 12, were 54000 ± 2000 and 51000 ± 2000, respectively. In order to investigate the specificity of these ligases, several compounds derived from their respective nucleotide substrates were prepared. In the case of the d-Glu-adding enzyme, DDP-MurNAc-l-Ala (DDP = dihydrouridine 5′-diphosphate) and P1-MurNAc-l-Ala were substrates of the reaction. In the case of the d-Ala-d-Ala-adding enzyme, only DDP-MurNAc-l-Ala-d-Glu(-meso-A2pm) was a subsrate; P1-MurNAc-l-Ala-d-Glu(-meso-A2pm) was neither a substrate nor an inhibitor. Concerning the amino acid site of the d-Glu-adding enzyme, even closely related analogues of d-glutamate hardly inhibited the reaction.

Abbreviations
A2pm

2,6-diaminopimelic acid

DDP

dihydrouridine 5′-diphosphate

Mur

muramic acid

NAc

N-acetyl

P1

1-phospho

Enzymes
 

UDP-N-acetylmuramoyl-l-alanine:d-glutamate ligase (ADP-forming), or d-Glu-adding enzyme (EC 6.3.2.9)

 

UDP-N-acetylmuramoyl-l-alanine-d-glutamate:meso-2,6-diaminopimelate ligase (ADP-forming), or meso-A2pm-adding enzyme (EC 6.3.2.13)

 

UDP-N-acetylmuramoyl-l-alanine-d-glutamate:L-lysine ligase (ADP-forming), or L-Lys-adding enzyme (EC 6.3.2.7)

 

UDP-N-acetylmuramoyl-l-alanine-d-glutamate:L-lysine ligase (ADP-forming), or L-Lys-adding enzyme (EC 6.3.2.7)

 

UDP-N-acetylmuramoyl-l-alanine-d-glutamyl-meso-2,6-diaminopimelate:d-alanyl-d-alanine ligase (ADP-forming), or d-Ala-d-Ala-adding enzyme (EC 6.3.2.15)

REFERENCES

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  2. Abstract
  3. REFERENCES
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