Literature summary for 2.4.99.16 extracted from

Elbein, A.D.; Pastuszak, I.; Tackett, A.J.; Wilson, T.; Pan, Y.T.
Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen (2010), J. Biol. Chem., 285, 9803-9812.

Search for more literature for 2.4.99.16

Inhibitors

Inhibitors	Comment	Organism	Structure
1,4-dideoxy-1,4-imino-D-arabinitol	-	Mycolicibacterium smegmatis
arsenate	-	Mycolicibacterium smegmatis
ATP	strong inhibition	Mycolicibacterium smegmatis
D-glucose 1-phosphate	slight inhibition	Mycolicibacterium smegmatis
D-glucose 6-phosphate	slight inhibition	Mycolicibacterium smegmatis
diphosphate	slight inhibition	Mycolicibacterium smegmatis
maltosaccharides	compete with glycogen for the transferred maltose	Mycolicibacterium smegmatis
additional information	no inhibition by isofagomine or acarbose	Mycolicibacterium smegmatis
phosphate	-	Mycolicibacterium smegmatis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics, overview	Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	Mycolicibacterium smegmatis	-	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	Mycolicibacterium smegmatis ATCC 14468	-	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	?

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	Q9RP48	-	-
Mycolicibacterium smegmatis ATCC 14468	Q9RP48	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme GMPMT 89fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography and gel filtration	Mycolicibacterium smegmatis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.76	-	purified enzyme, pH 7.0, 37°C	Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	-	Mycolicibacterium smegmatis	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose	Mycolicibacterium smegmatis	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	r
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	-	Mycolicibacterium smegmatis ATCC 14468	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n	liver, oyster, or mycobacterial glycogens are the best acceptors, amylopectin has good activity, but amylose is a poor acceptor. GMPMT also appears to be able to catalyze arsenolysis of glycogen with release of malto-oligosaccharides or at least maltotriose	Mycolicibacterium smegmatis ATCC 14468	phosphate + [(1->4)-alpha-D-glucosyl]n+2	-	r
additional information	GMPMT requires a high-molecular weight alpha-1,4-glucan as the acceptor. The enzyme can also transfer maltosyl units to maltosaccharides, e.g. maltotetraose to maltohexaose, overview	Mycolicibacterium smegmatis	?	-	?
additional information	GMPMT requires a high-molecular weight alpha-1,4-glucan as the acceptor. The enzyme can also transfer maltosyl units to maltosaccharides, e.g. maltotetraose to maltohexaose, overview	Mycolicibacterium smegmatis ATCC 14468	?	-	?

Synonyms

Synonyms	Comment	Organism
alpha1,4-glucan:maltose-1-P maltosyltransferase	-	Mycolicibacterium smegmatis
GMPMT	-	Mycolicibacterium smegmatis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Mycolicibacterium smegmatis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Mycolicibacterium smegmatis

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the last step in the conversion of trehalose to glycogen transfering maltose from maltose 1-phosphate to glycogen. Trehalose synthase, maltokinase, and GMPMT represent an additional pathway of glycogen synthesis using trehalose as the source of glucose	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)