Biotransformation of 2-keto-4-hydroxybutyrate via aldol condensation using an efficient and thermostable carboligase from Deinococcus radiodurans

Bioresources and Bioprocessing

Table 1 Biochemical properties of the characterized pyruvate aldolases

Enzyme	Temperature (°C)	pH	Specific activity (μmol mg⁻¹ min⁻¹)	Formaldehyde			Pyruvate			References
Enzyme	Temperature (°C)	pH	Specific activity (μmol mg⁻¹ min⁻¹)	k_cat (min⁻¹)	K_m (mM)	k_cat/K_m (min⁻¹ mM⁻¹)	k_cat (min⁻¹)	K_m (mM)	k_cat/K_m (min⁻¹ mM⁻¹)	References
MBP-EcYfaU	25^a	7.0^a	10	NR	NR	NR	NR	NR	NR	Hernandez et al. (2017)
MBP-EcYfaU	25^a	7.0^a	60 ± 1^b	113	24	4.71	113	209	0.54	Bosch et al. (2021)
EcKHB	30^a	7.0^a	1.62 ± 0.11^c	NR	NR	NR	NR	NR	NR	Wang et al. (2019)
BtKHG	30^a	7.0^a	0.11 ± 0.01^c	NR	NR	NR	NR	NR	NR	Wang et al. (2019)
HsKHG	30^a	7.0^a	0.10 ± 0.01^c	NR	NR	NR	NR	NR	NR	Wang et al. (2019)
RnKHG	30^a	7.0^a	0.08 ± 0.01^c	NR	NR	NR	NR	NR	NR	Wang et al. (2019)
MBP-PaADL^WT	45	9.0	5.87 ± 0.05	271	45	10	255	37	6.8	Jeong et al. (2023)
MBP-PaADL^V121A/L241A	45	9.0	7.54 ± 0.05	398	65	11	453	52	8.8	Jeong et al. (2023)
MBP-DrADL	50	8.0	46.3 ± 0.36	11,845	8.79	1347	7670	4.06	1889	This study

NR: not reported
^aThe enzyme activities were assayed each condition
^bSpecific activity of MBP-EcYfaU was determined with retro-aldol consultation activity
^cEnzyme activities of these enzymes were measured using resting cells expressing each enzyme (unit = μmol min⁻¹ OD⁻¹ mg⁻¹)