Products

Bacterial cell wall synthesis enzyme assays

The following high throughput assays for enzymes in the bacterial cell wall synthesis pathway are available

for drug discovery.

Bacterial D-Alanine : D-Alanine ligase assay

D-Alanine-D-Alanine is one of the building blocks in peptidoglycan biosynthesis in bacteria.  This dipeptide

is generated by ligation between two D-Alanine molecules catalyzed by D-Alanine : D-Alanine ligase.  The

ligation reaction is coupled to the hydrolysis of ATP forming ADP and inorganic phosphate.

The E. coli D-Alanine : D-Alanine Ligase Assayis based on measurement of the inorganic phosphate

generated from the D-Alanine : D-Alanine ligation reaction.  The inorganic phosphate is detected by light

absorbance at 650 nm. The assay reactions and detection can be performed by using 384-well or 96-well

assay plates. Alternatively, the assay reaction can be carried out in Eppendorf tubes and the signal is

measured using a cuvette. The high throughput assay can be used for screening inhibitors of E.coli D-

Alanine : D-Alanine ligase in drug discovery research.  It may also be used for characterization of E.coli D-

Alanine : D-Alanine ligase.

Bacterial MurA Assays

MurA or UDP-N-acetylglucosamine enolpyruvyl transferase catalyzes the first committed step in

peptidoglycan biosynthesis in bacteria.  It is an essential enzyme and attractive target for anti-bacterial drug

discovery. MurA transfers enolpyruvate from phosphoenolpyruvate (PEP) to uridine diphospho-N-

acetylglucosamine (UNAG) generating enolpyruvyl-UDPN-acetylglucosamine (EP-UNAG) and inorganic

phosphate.

The Bacterial MurA Assay is based on measurement of the inorganic phosphate generated from the MurA

reaction.  The inorganic phosphate is detected by light absorbance at 650 nm. The assay reactions and

detection can be performed by using 384-well or 96-well assay plates. Alternatively, the assay reaction can

be carried out in Eppendorf tubes and the signal is measured using a cuvette. The high throughput assay

can be used for screening inhibitors of bacterial MurA in drug discovery research.  It may also be used for

characterization of bacterial MurA.

Bacterial MurC Assays

MurC or UDP-N-acetylmuramic acid:L-alanine ligase is the first of four paralogous amino acid-adding

enzymes in the pathway of peptidoglycan biosynthesis in bacteria. It is an essential enzyme and attractive

target for anti-bacterial drug discovery. MurC catalyzes the addition of L-alanine onto the nucleotide

precursor UDP-MurNAc generating UDP-MurNAc-L-Ala. The ligation reaction is coupled to the hydrolysis of

ATP forming ADP and inorganic phosphate.

The Bacterial MurC Assay is based on measurement of the inorganic phosphate generated from the MurC

reaction.  The inorganic phosphate is detected by light absorbance at 650 nm. The assay reactions and

detection can be performed by using 384-well or 96-well assay plates. Alternatively, the assay reaction can

be carried out in Eppendorf tubes and the signal is measured using a cuvette. The high throughput assay

can be used for screening inhibitors of bacterial MurC in drug discovery research.  It may also be used for

characterization of bacterial MurC.

Bacterial MurD Assays

MurD is a D-Glutamic acid-adding enzyme in the pathway for bacterial cell-wall peptidoglycan synthesis. It

is an essential enzyme and attractive target for anti-bacterial drug discovery. MurD catalyses the addition of

D-glutamic acid to UDP-MurNAc-L-Ala, generating UDP-MurNAc-dipeptide. The ligation reaction uses ATP

hydrolysis as an energy source forming ADP and inorganic phosphate.

The Bacterial MurD Assay is based on measurement of the inorganic phosphate generated from the MurD

reaction.  The inorganic phosphate is detected by light absorbance at 650 nm. The assay reactions and

detection can be performed by using 384-well or 96-well assay plates. Alternatively, the assay reaction can

be carried out in Eppendorf tubes and the signal is measured using a cuvette. The high throughput assay

can be used for screening inhibitors of bacterial MurD in drug discovery research.  It may also be used for

characterization of bacterial MurD.

Bacterial MurE Assays

MurE or UDP-MurNAc-tripeptide ligase is the third amino acid-adding enzymes in the pathway of

peptidoglycan biosynthesis in bacteria . It is an essential enzyme and attractive target for anti-bacterial drug

discovery. MurE catalyses the addition of lysine or meso-diaminopimelic acid (DAP) into the MurD product

UDP-MurNAc-dipeptide in bacteria generating the UDP-MurNAc-tripeptide. The ligation reaction is coupled to

the hydrolysis of ATP forming ADP and inorganic phosphate.

The Bacterial MurE Assay is based on measurement of the inorganic phosphate generated from the MurE

reaction.  The inorganic phosphate is detected by light absorbance at 650 nm. The assay reactions and

detection can be performed by using 384-well or 96-well assay plates. Alternatively, the assay reaction can

be carried out in Eppendorf tubes and the signal is measured using a cuvette. The high throughput assay

can be used for screening inhibitors of bacterial MurE in drug discovery research.  It may also be used for

characterization of bacterial MurE.

Bacterial MurF assays

MurF is the enzyme that catalyzes the last step in synthesis of UDP-MurNAc-pentapeptide in the pathway of

peptidoglycan biosynthesis in bacteria. It is an essential enzyme and attractive target for anti-bacterial drug

discovery. MurF adds a dipeptide D-Ala-D-Ala onto the MurE product UDP-MurNAc-tripeptide.  The ligation

reaction is coupled to the hydrolysis of ATP forming ADP and inorganic phosphate.

The Bacterial MurF Assay is based on measurement of the inorganic phosphate generated from the MurF

reaction.  The inorganic phosphate is detected by light absorbance at 650 nm. The assay reactions and

detection can be performed by using 384-well or 96-well assay plates. Alternatively, the assay reaction can

be carried out in Eppendorf tubes and the signal is measured using a cuvette. The high throughput assay

can be used for screening inhibitors of bacterial MurF in drug discovery research.  It may also be used for

characterization of bacterial MurF.