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. Author manuscript; available in PMC: 2012 Feb 22.
Published in final edited form as: Biochemistry. 2011 Jan 25;50(7):1247–1254. doi: 10.1021/bi101642d

Table 2.

Substrate specificity of PaMTIP.

Substrate kcat (s−1) Km or Ki (µM) kcat/Km (M−1s−1)
MTI 4.8 ± 0.2 2.6 ± 0.4 (1.8 ± 0.3) × 106
MTA a N/A 70 ± 20 N/A
inosine 0.57 ± 0.04 90 ± 20 (6 ± 1) × 103[300] b
adenosine 0.0549 ± 0.0005 23 ± 1 (2.4 ± 0.1) × 103[750] b
a

MTA is not a substrate of PaMTIP. Ki is used instead of Km for MTA.

b

Numbers in [] are fold decreases of kcat/Km in comparion with those of MTI.

c

Values are ± S.E.