TABLE 3.
Organism | Protein | Gene | 3-Hydroxybutyryl-CoA |
Acetoacetyl-CoA |
References | ||||
Vmax/kcat | Km | kcat/Km | Vmax/kcat | Km | kcat/Km | ||||
Nitrosopumilus maritimus SCM1 | HBDH | Nmar_1028 | 98.6/74 (2 mM NAD) 76.1/57 (0.5 mM NAD) | 0.019 (2 mM NAD)0.017 (0.5 mM NAD) | 3,877 (2 mM NAD) 3,344 (0.5 mM NAD) | 144.8/108 | 0.026 | 4,160 | This work |
Metallosphaera sedula DSM 5348 | HBDH | Msed_1423 | 96/75(0.5 mM NAD) | 0.005 | 14,957 | NR | NR | NR | Liu et al., 2020 |
CCH/HBDH | Msed_0399 | 76/90a 22.6/19a 27.6/33a | 0.12 0.060.2 | 748 445163 | NR | NR | NR | Ramos-Vera et al., 2011; Hawkins et al., 2014; Liu et al., 2020 | |
Ignicoccus hospitalis | CCH/HBDH | Igni_1058 | 117/152 | 0.086 | 1,800 | NR | NR | NR | Flechsler et al., 2021 |
Cupriavidus necator H16 | HBDH/enoyl-CoA hydrataseb | H16_A0461 | NR | NR | NR | 149/216 | 0.048 | 4,500 | Volodina and Steinbüchel, 2014 |
HBDH | RePaaH1 | NR | NR | NR | 85.4/46 | 0.018 | 2,530 | Kim J. et al., 2014 | |
Clostridium butyricum | HBDH | CbHBD | NR | NR | NR | 56.8/29 | 0.028 | 1,035 | Kim E. J. et al., 2014 |
Caenorhabditis elegans Bristol N2 | HADH | cHAD | NR | NR | NR | 78/45 | 0.072 | 600 | Xu et al., 2014 |
Mycobacterium tuberculosis H37Rv | HBDH | FadB2 | 0.19/0.096 | 0.0435 | 2 | 0.13/0.065 | 0.0656 | 1 | Taylor et al., 2010 |
Escherichia coli ATCC 11775 | Fatty acid oxidation complex | ? | NR | NR | NR | 64/288 | 0.066 | 4,364 | Binstock and Schulz, 1981 |
Mycolicibacterium smegmatis ATCC 14468 | HADH | ? | NR | NR | NR | 12.5/10 | 0.036 | 291 | Shimakata et al., 1979 |
Homo sapiens | Short-chain HADH I | SCHAD I | NR/119 | 0.0225 | 5,290 | NR/1,287 | 0.0166 | 77,500 | Filling et al., 2008 |
Short-chain HADH II | SCHAD II | NR/4.83 | 0.0852 | 58 | NR/23.8 | 0.0257 | 927 | Filling et al., 2008 | |
Short chain L-HADH | rSCHADH6 | NR | NR | NR | 459/252 | 0.0187 | 13,500 | Barycki et al., 1999 | |
Short chain L-HADH | SCHAD | NR/0.011 | 0.043 | 0.26 | NR | NR | NR | He et al., 1999 | |
L-HADH | HBHAD | NR | NR | NR | NR/37 | 0.089 | 416 | He et al., 1998 | |
Rattus norvegicus | HADH | HAD | NR | NR | NR | 976/569 | 0.044 | 13,000 | Liu et al., 2004 |
HADH I | ? | 270/144 | 0.0699 | 2,060 | 820/437 | 0.0169 | 25,878 | Osumi and Hashimoto, 1980 | |
HADH II | ? | 15.6/20 | 0.0422 | 474 | 23.5/30 | 0.0397 | 760 | Osumi and Hashimoto, 1980 | |
Sus scrofa | L-HADH | HAD | NR | NR | NR | NR/330 | 0.003 | 110,000 | He and Yang, 1998 |
L-HADH | ? | 39/21 | 0.0072 | 2,889 | 230/123 | 0.0118 | 10,395 | He et al., 1989 | |
L-HADH | ? | NR | NR | NR | 426/227 | 0.06 | 3,787 | Noyes and Bradshaw, 1973 |
Vmax, U mg–1 protein; kcat, s–1; Km, mM. (S)-3-hydroxybutyryl-CoA dehydrogenase, HBDH; crotonyl-CoA hydratase, CCH; 3-hydroxyacyl-CoA dehydrogenase, HADH?, unknown; NR, not reported. aThe Vmax values are normalized to 75°C based on the assumption that a 10°C rise in temperature doubles the reaction rate. bSpecific activity with crotonyl-CoA was 98 U mg–1.