Literature summary for 5.4.99.11 extracted from

Watzlawick, H.; Mattes, R.
Gene cloning, protein characterization, and alteration of product selectivity for the trehalulose hydrolase and trehalulose synthase from "Pseudomonas mesoacidophila" MX-45 (2009), Appl. Environ. Microbiol., 75, 7026-7036.

Search for more literature for 5.4.99.11

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli JM109 cells	Paraburkholderia acidicola

Protein Variants

Protein Variants	Comment	Organism
D442N	the mutant favors the transfer reaction with an isomer preference for isomaltulose	Paraburkholderia acidicola
R311C	the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production	Paraburkholderia acidicola

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
30	-	Trehalulose	wild type enzyme	Paraburkholderia acidicola
30	-	isomaltulose	wild type enzyme	Paraburkholderia acidicola
40	-	isomaltulose	mutant enzyme R311C	Paraburkholderia acidicola
43	-	D-glucose	mutant enzyme R311C	Paraburkholderia acidicola
79	-	Trehalulose	mutant enzyme R311C	Paraburkholderia acidicola
100	-	D-glucose	mutant enzyme D442N	Paraburkholderia acidicola
185	-	Trehalulose	mutant enzyme D442N	Paraburkholderia acidicola
240	-	D-glucose	wild type enzyme	Paraburkholderia acidicola
500	-	isomaltulose	mutant enzyme D442N	Paraburkholderia acidicola

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Paraburkholderia acidicola	-	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
55000	-	SDS-PAGE	Paraburkholderia acidicola
63750	-	MALDI-TOF mass spectrometry	Paraburkholderia acidicola
64290	-	mature MutB, calculated from amino acid sequence	Paraburkholderia acidicola

Organism

Organism	UniProt	Comment	Textmining
Paraburkholderia acidicola	Q2PS28	-	-
Paraburkholderia acidicola MX-45	Q2PS28	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Paraburkholderia acidicola

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
sucrose	MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)	Paraburkholderia acidicola	isomaltulose + trehalulose + D-glucose	-	r
sucrose	MutB catalyzes the isomerization of sucrose to mainly trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose)	Paraburkholderia acidicola MX-45	isomaltulose + trehalulose + D-glucose	-	r

Synonyms

Synonyms	Comment	Organism
MutB	-	Paraburkholderia acidicola
sucrose isomerase	-	Paraburkholderia acidicola
Trehalulose synthase	-	Paraburkholderia acidicola

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.7	-	isomaltulose	mutant enzyme R311C	Paraburkholderia acidicola
11.5	-	Trehalulose	mutant enzyme R311C	Paraburkholderia acidicola
15	-	D-glucose	wild type enzyme	Paraburkholderia acidicola
32.5	-	D-glucose	mutant enzyme R311C	Paraburkholderia acidicola
44	-	D-glucose	mutant enzyme D442N	Paraburkholderia acidicola
241	-	Trehalulose	mutant enzyme D442N	Paraburkholderia acidicola
258	-	isomaltulose	wild type enzyme	Paraburkholderia acidicola
1144	-	Trehalulose	wild type enzyme	Paraburkholderia acidicola
1947	-	isomaltulose	mutant enzyme D442N	Paraburkholderia acidicola

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
0.042	-	isomaltulose	mutant enzyme R311C	Paraburkholderia acidicola
0.06	-	D-glucose	wild type enzyme	Paraburkholderia acidicola
0.15	-	Trehalulose	mutant enzyme R311C	Paraburkholderia acidicola
0.44	-	D-glucose	mutant enzyme D442N	Paraburkholderia acidicola
0.76	-	D-glucose	mutant enzyme R311C	Paraburkholderia acidicola
1.3	-	Trehalulose	mutant enzyme D442N	Paraburkholderia acidicola
3.9	-	isomaltulose	mutant enzyme D442N	Paraburkholderia acidicola
8.6	-	isomaltulose	wild type enzyme	Paraburkholderia acidicola
36	-	Trehalulose	wild type enzyme	Paraburkholderia acidicola

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Release 2023.1 (January 2023)