Literature summary for 5.4.99.16 extracted from

Zhu, Y.; Wei, D.; Zhang, J.; Wang, Y.; Xu, H.; Xing, L.; Li, M.
Overexpression and characterization of a thermostable trehalose synthase from Meiothermus ruber (2010), Extremophiles, 14, 1-8.

Search for more literature for 5.4.99.16

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli Rosetta gami (DE3) cells	Meiothermus ruber

Inhibitors

Inhibitors	Comment	Organism	Structure
Al3+	complete inhibition at 2 mM	Meiothermus ruber
Ca2+	about 10% residual activity at 10 mM	Meiothermus ruber
Co2+	about 5% residual activity at 10 mM	Meiothermus ruber
Cu2+	complete inhibition at 2 mM	Meiothermus ruber
D-glucose	in the presence of 10 mM D-glucose, TreS shows a 3.6fold increase in Km and a nearly unchanged Vmax for maltose, implying that D-glucose is a competitive inhibitor of TreS	Meiothermus ruber
Fe2+	complete inhibition at 2 mM	Meiothermus ruber
Mn2+	about 10% residual activity at 10 mM	Meiothermus ruber
Ni2+	about 10% residual activity at 10 mM	Meiothermus ruber
Zn2+	complete inhibition at 2 mM	Meiothermus ruber

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
98.9	-	alpha,alpha-trehalose	-	Meiothermus ruber
126.2	-	maltose	-	Meiothermus ruber

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
110000	-	SDS-PAGE	Meiothermus ruber

Organism

Organism	UniProt	Comment	Textmining
Meiothermus ruber	B1PK99	-	-
Meiothermus ruber CBS-01	B1PK99	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-NTA column chromatography	Meiothermus ruber

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
maltose	the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate	Meiothermus ruber	alpha,alpha-trehalose	TreS also has a weak hydrolytic property with D-glucose as the byproduct	r
maltose	the enzyme has a 2fold higher catalytic efficiency (kcat/Km) for maltose than for trehalose indicating maltose as the preferred substrate	Meiothermus ruber CBS-01	alpha,alpha-trehalose	TreS also has a weak hydrolytic property with D-glucose as the byproduct	r

Synonyms

Synonyms	Comment	Organism
Trehalose synthase	-	Meiothermus ruber
TreS	-	Meiothermus ruber

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
50	-	-	Meiothermus ruber

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
60	-	the enzyme maintains very high activity (above 90%) at 60°C for 5 h	Meiothermus ruber

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
68.9	-	alpha,alpha-trehalose	-	Meiothermus ruber
147	-	maltose	-	Meiothermus ruber

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	-	-	Meiothermus ruber

pH Range

pH Minimum	pH Maximum	Comment	Organism
6	7	-	Meiothermus ruber

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
4	8	the enzyme can maintain very high activity (above 90%) at pH 4.0-8.0 for 5 h, below pH 5.0 the enzyme shows no activity	Meiothermus ruber

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
3.76	-	D-glucose	-	Meiothermus ruber

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.7	-	alpha,alpha-trehalose	-	Meiothermus ruber
1.17	-	maltose	-	Meiothermus ruber

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Release 2023.1 (January 2023)