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. 2021 Jul 5;12:712030. doi: 10.3389/fmicb.2021.712030

TABLE 3.

Catalytic properties of various so-far-characterized 3-hydroxyacyl-CoA dehydrogenases toward 3-hydroxybutyryl-CoA and/or acetoacetyl-CoA.

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 mg1 protein; kcat, s1; 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 mg1.