TABLE 3.
Substrate analysis of YfkJ and YwlE
| Substrateb | Activity of enzyme (Miller units)a
|
|||
|---|---|---|---|---|
| YfkJ | YwlE | LMPTP-A | LMPTP-B | |
| pNPP | 100 | 100 | 100 | 100 |
| FTATEGQpYQPQP | 0 | 18.1 | 61.7 | 17.1 |
| FTATEGQpYQPIP | 0 | 7.6 | 41.3 | 12.6 |
| FTATEGQpYQEIP | 0.4 | 31.8 | 65.3 | 18.8 |
| FTATEGQpYEEIP | 0.1 | 36.9 | 43.2 | 12.1 |
| RRApSVA | 0 | 0 | 2.9 | 4.0 |
| KRpTIRR | 0 | 0 | 3.8 | 1.6 |
| p-Tyr | 2.3 | 13.2 | 82.7 | 26.6 |
| p-Ser | 0 | 3.6 | 6.2 | 3.8 |
| p-Thr | 0 | 0 | 0 | 0 |
| α-Naphthyl phosphate | 0.6 | 3.5 | 4.5 | 1.2 |
| β-Naphthyl phosphate | 21.7 | 69.9 | 102.4 | 98.1 |
| Glucose-1-phosphate | 0 | 20.8 | 7.3 | 5.4 |
| Glucose-6-phosphate | 0 | 0 | 1.4 | 0 |
| Ribose-5-phosphate | 0 | 0 | 8.8 | 0 |
| β-Glycerol phosphate | 0 | 0 | 0.4 | 0 |
| Pyridoxal 5′ Phosphate | 0 | 0 | 0 | 0 |
| IMP | 0.9 | 4.7 | 2.1 | 1.2 |
| ATP | 0 | 0 | 0.5 | 0 |
| ADP | 0 | 0 | 0 | 0 |
| AMP | 0.7 | 2.1 | 2.2 | 0.1 |
| GMP | 0.6 | 2.5 | 4.2 | 0 |
| CMP | 0.7 | 2.3 | 2.8 | 0.5 |
| UMP | 0 | 0 | 1.5 | 1.7 |
a
Values are relative activities of B. subtilis His-YfkJ and His-YwlE and of human GST-LMPTP-A and GST-LMPTP-B.
b
The reaction buffer was 50 mM MES (pH 5.5) with 1 mM DTT for His-YwlE or 50 mM Na citrate (pH. 6.0) for the other enzymes. Substrates were present at a 1 mM concentration. pY, phosphotyrosine; pS, phosphoserine; pT, phosphothreonine.