Table 1.

Biochemical characterization of bacterial GH37 trehalases.

Enzyme	VMAX (μM min−1)	KM (mM)	KCAT (min−1)	Specific activity (μmol min−1 mg−1)	pH	Temp (°C)	Source
E. coli TreA	0.012	0.41	1.2 x 103	6.6 x 101	5.5	37	(Gibson et al. 2007)
E. coli TreF	54	1.9	N/A	6.0 x 101	6	N/A	(Horlacher et al. 1996)
E. cloacae TreA	200	1.47	6.3 x 103	1.4 x 103	5	55	(Adhav et al. 2019)
N. punctiforme TreH	N/A	18	N/A	2.5 x 10−2	7.5	N/A	(Yoshida and Sakamoto 2009)
R. marinus TreH	81	0.16	N/A	1.3 x 101	6.5	88	(Jorge et al. 2007)
Zunongwangia sp. TreZ	N/A	0.99	1.6 x 104 5795	2.6 x 102	6	50	(Cheng et al. 2016)
X. citri sp. citri TreA	55.038	0.077	N/A	5.5 x 101	8	25	(Alexandrino et al. 2016)
C. japonicus Tre37A	N/A	N/A	N/A	7.3 x 103	6	20-30	(Garcia et al. 2020)