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. 2022 Nov 10;10(6):e03818-22. doi: 10.1128/spectrum.03818-22

TABLE 3.

Comparison of kinetic properties of glucose-6-phosphate dehydrogenases

Organism G6P with fixed conc. of NADP+
G6P with fixed conc. of NAD+
NADP+ with fixed conc. of G6P
NAD+ with fixed conc. of G6P
kcat/Km(NADP+)/
kcat/Km(NAD+)
Quarternary structure Subunit mol. wt. (kDa) pH optima References
Km a kcat kcat/Km SSb Km kcat kcat/Km SSb Km kcat kcat/Km Km kcat kcat/Km
P. bharatica CSV86T (A)c 1827 191 0.10 S (1.84) 1697 230 0.16 S (2.1) 110 187 1.7 366 306 0.86 2 Homotetramer 55.8 8.25 Current study
P. bharatica CSV86T (B) 5827 NAd NA M 9968 NA NA M 67 NA NA 577 NA NA NA NA 51.5 6.5
P. bharatica CSV86T (C) 1940 11.4 0.0056 M 364 11.4 0.03 M 18 8.5 0.48 3100 11.9 0.004 123 Homotetramer 57.5 8.25
T. maritima 200 35000 175 M NA NA NA NA 40 35000 875 12000 11000 0.92 955 Homodimer 60 7.4 29
E. coli NA NA NA NA NA NA NA NA 7.5 174 23.2 5090 288 0.06 410 NA NA 8.2 18
G. oxydans 280 44 0.16 M NA NA NA NA 26 43 1.6 740 43 0.06 28 Homodimer 54.5 7 42
L. mesenteroids 114 523 4.6 M 69 1125 16.3 M 8 522 65.3 162 1125 6.9 9.4 Homodimer - 7.6 39
A. aeolicus 40°C 15 NA NA M 58 NA NA M 9.1 47 5.1 230 58 0.25 20 Homodimer 55 7 41
A. aeolicus 70°C 63 NA NA M 180 NA NA M 161 894 5.6 2096 2012 0.96 5.8
Z. mobilis NA NA NA M NA NA NA M 40 338 8.5 210 589 2.8 3 Homotetramer 52 8 28
P. fluorescens 2700 NA NA S (1.65) 2330 NA NA S (1.59) 360 1117 3.1 150 1383 9.2 0.34 NA NA 8.9 15
P. putida KT2440 (A) 946 NA NA M 1137 NA NA M 14 102 7.3 127 227 1.8 4.1 NA NA 8 8
P. putida KT2440 (B) 190 NA NA M 291 NA NA M 165 113 0.68 151 120 0.8 0.86 NA NA 8 14
P. putida KT2440 (C) 944 NA NA M 2030 NA NA M 3.2 0.54 0.17 9500 0.77 8.1 × 10−5 2082 NA NA 8
P. aeruginosa (A) 499 NA NA S (1.99) 1146 NA NA S (2.38) 57 540 9.5 527 1017 1.9 4.9 Homotetramer or octamer 55 8 20
A. vinelandii 530 NA NA S (1.66) 690 NA NA S (1.76) 50 36.7 0.73 220 91 0.41 1.8 Homotetramer 52 8.5 16
a

Km, μM; kcat, s−1; kcat/Km, μM−1 s−1.

b

SS, substrate saturation profile: S, sigmoidal saturation profile with Hill’s coefficient (n) value in the bracket indicating the allosteric nature of enzyme; M, Michaelis-Menten hyperbolic saturation profile.

c

Zwf A, B, or C isozymes.

d

NA, data not available.