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. Author manuscript; available in PMC: 2016 Sep 26.
Published in final edited form as: Curr Med Chem. 2011;18(13):1909–1918. doi: 10.2174/092986711795590129

Table 1.

Steady state kinetic parameters of IMPDH from various organisms.

IMPDH kcat
(s−1)
Km
IMP
(μM)
Km
NAD+
(μM)
Kii NAD+
(mM)
Ki MPA
(nM)
Human type I 1.2-1.8a 14-18a 42-70a 2.0b 11-33c
Human type II 0.4-1.4d 4-9d 6-32d 0.59e 7-14f
Aerobacter aerogenes t n.d. 60 800 n.d. n.d.
Borellia burgdorferi g 2.6 30 1100 2.3 8,000
Cryptosporidium parvum h 3.3 29 150 2.9 9,300
Escherichia coli 13i 61i 2000i 2.8i ~20,000j
Helicobacter pylori k 3.0 18 73 1.7 n.d.
Mycobacterium tuberculosis l 0.53 78 1000 5.0 62,000
Streptococcus pyogenes m 24 62 1180 n.d. >10,000
Tritrichomonas foetus n 1.9g 1.7g 150g 6.8g 9,000g

n.d., no data. Assay buffers are generally similar, but temperature varies between 25-37 degrees C. Values of kcat are reported per active site, not per tetramer. Note that while C. parvum and T. foetus are protozoan parasites, their IMPDHs are most similar bacterial enzymes, suggesting that the genes where obtained by horizontal transfer.

a

[80, 81] [82];

b

[82];

c

[80, 81];

d

[80, 81, 83];

e

[83];

f

[57, 80, 84];

g

[85];

h

[66];

i

[86];

j

N. Benfield and L. Hedstrom, unpublished data;

k

[24];

l

[62];

m

[78];

n

[87].