. Author manuscript; available in PMC: 2012 Mar 29.

Published in final edited form as: Biochemistry. 2011 Feb 18;50(12):2339–2356. doi: 10.1021/bi1014453

Table 5.

Kinetic Properties of RPTPA against pY Peptides

Entry No.	Peptide Sequence	k_cat (s⁻¹)	K_M (mM)	k_cat/K_M (mM⁻¹ s⁻¹)
1	EADTApYAA^a	26 ± 1	1.4 ± 0.1	19
2	ASSDDpYAA^a	ND	ND	13
3	WDEDFpYSASA^a	ND	ND	69
4	ARKRIpYAA^a	39 ± 1	0.49 ± 0.03	80
5	RRISTpYAA^a	49 ± 3	1.2 ± 0.1	41
6	SASASpYSASA^a	23 ± 4	0.53 ± 0.15	43
7	AAAAApYEEVH^a	ND	ND	39
8	AAAAApYRHRR^a	30 ± 2	2.6 ± 0.2	12
9	TATEPQpYQPGENL^b	9.7 ± 0.2	1.07 ± 0.03	9.1
10	TSTEPQpYQPGENL^b	8.9 ± 0.5	1.16 ± 0.14	7.7
11	LIEDNEpYTARQGA^b	8.3 ± 0.2	0.77 ± 0.02	11
12	Phenyl phosphate	ND	ND	0.020
13	pNPP	0.54 ± 0.28	2.7 ± 0.3	0.19

These peptides contained an N-terminal acetyl group and a C-terminal amide.

Data from ref. 20. Data reported represented the mean ± SD from three or more independent sets of experiments.