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. Author manuscript; available in PMC: 2020 Aug 6.
Published in final edited form as: Biochemistry. 2019 Jul 26;58(31):3340–3353. doi: 10.1021/acs.biochem.9b00326

Table 2.

Turnover Numbers for Substrates with YdjI and DHAPa

substrate expected
product		 apparent kcat
(s−1)b 		MW
(M)		 found MW (M −
H)−
 3  34   0.40 ± 0.05 243.99 242.99
 5  35   2.2 ± 0.2 244.03 243.03
 6  36   4.8 ± 0.6 244.03 243.03
 9/10  37/38   0.50 ± 0.02 274.00 273.00
 13  40   0.64 ± 0.03 242.01 241.01
 14  41   0.71 ± 0.06 290.03 289.03
 15  42   0.48 ± 0.04 290.03 289.03
 17  43   0.68 ± 0.04 304.01 303.01
 20  44   0.66 ± 0.04 370.00 369.00
 25  45   3.0 ± 0.3 334.02 333.02
 26  46   2.3 ± 0.2 334.02 333.02
 28  47 >0.7c 334.02 333.02
 29  48   0.50 ± 0.04 400.01 399.01
 30  49   1.60 ± 0.09 400.01 399.01
 32  50   0.050 ± 0.004 364.03 363.03
 33  51   1.8 ± 0.1 364.03 363.03
a

Reactions were monitored by 31P NMR spectroscopy and quantified by integration with an internal phosphate standard.

b

Errors were calculated from the standard deviation of the fitting results as described.

c

Overlap between substrate and product peaks prevented accurate integrations. The value reported is a lower limit based on the amount of product formed in 30 min and corrected for enzyme concentration.