Category:Team EKSUtopaz

Figure 2 and Table 1 show that gp61 has lytic activity against S. aureus.

It also demostrates that this activity is localized to two domains (amino acids 1-150 and 401-624) of the polypeptide. Figure 4 shows that gp61 is located at the tail tip.

FIGURE 1 shows that the lysozyme-like domain (TG1) of Tape Measure Protein (TMP) of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has peptidoglycan muramidase activity and is most likely a muramidase that can digest MurNAc-GlcNAc linkages.

The lytic activity TG1 protein against S. aureus is shown in Figure 2.

Figure 3 and 5show ATP activity and complementation of Samonella Typhimurium pyridine nucleotide auxotroph by the nadV+clone (pZL405nadV+)

Figure 7 (explanation from the manuscript).

Figure Title: Substrate specificity of the KVP40 NatV Nudix pyrophosphatase.

A) Activity was measured in the phosphate release assay using 1.5 mM of substrate and

50 pmole NatV-His6 present in reactions incubated at 37°C. Values shown are averages from two assays. Stoichiometry of phosphate per substrate is 1:1.

B) Mass spectrometry analysis of KVP40 NatV 754 Nudix hydrolase substrate specificity. Specific activity was obtained with 1.5 mM substrate and 1 μg NatV, incubated at 37°C. Values are averages from duplicate assays (triplicate for ADP-ribose). The specific activity on ADP-ribose was 0.6 μmole AMP sec^-1 µg^-1 NatV-His6.

Figure 7 shows substrate specificity of NatV Nudix hydrolase as measured by Pi released from the respective substrate. At 37 degree centigrade, the preferred substrate are ADP-ribose, NAD+ and NADH with little differences in activity between them.

The stoichiometry of Pi from all of these Nudix hydrolase reactions is 1:1, most yielding an AMP. In reactions where AMP could be directly measured using mass spectrophotometer, ADP-ribose was also preferred substrate, with NAD+, NADH, with FAD showing reactivity but not at a lower rate

figure S2 shows that SAP-2_gp10 is a homologue of Andhra_gp10(confirmed by a BLASTP of Andhra_gp10).

Figure 2 shows that the wildtype Andhra_gp10 is a peptidase with a CHAP(cysteine, histidine-dependent amidohydrolases/peptidases) domain and mutations of the cysteine(C354A) and histidine (H420A) in the CHAP domain abrogate the peptidase activity of Andhra_gp10. Currently there is no UNIPROT ID for Andhra_gp10. Hence, its Genbank Accession Number(AQT27832) has been included in the with/from field.