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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.1.175 synthesis enzymatic synthesis of maltose 1-phosphate Mycolicibacterium smegmatis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.99.16 1,4-dideoxy-1,4-imino-D-arabinitol
-
 Mycolicibacterium smegmatis
2.4.99.16 arsenate
-
 Mycolicibacterium smegmatis
2.4.99.16 ATP strong inhibition Mycolicibacterium smegmatis
2.4.99.16 D-glucose 1-phosphate slight inhibition Mycolicibacterium smegmatis
2.4.99.16 D-glucose 6-phosphate slight inhibition Mycolicibacterium smegmatis
2.4.99.16 diphosphate slight inhibition Mycolicibacterium smegmatis
2.4.99.16 maltosaccharides compete with glycogen for the transferred maltose Mycolicibacterium smegmatis
2.4.99.16 additional information no inhibition by isofagomine or acarbose Mycolicibacterium smegmatis
2.4.99.16 phosphate
-
 Mycolicibacterium smegmatis

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.175 Mg2+ required Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.99.16 Mycolicibacterium smegmatis Q9RP48
-
-
2.4.99.16 Mycolicibacterium smegmatis ATCC 14468 Q9RP48
-
-
2.7.1.175 Mycolicibacterium smegmatis
-
-
-
2.7.1.175 Mycolicibacterium smegmatis ATCC 14468
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.99.16 0.76
-
 purified enzyme, pH 7.0, 37°C Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
-
 Mycolicibacterium smegmatis phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?
2.4.99.16 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
2.4.99.16 alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
-
 Mycolicibacterium smegmatis ATCC 14468 phosphate + [(1->4)-alpha-D-glucosyl]n+2
-
 ?
2.4.99.16 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
2.4.99.16 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 ?
-
 ?
2.4.99.16 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 ?
-
 ?
2.7.1.175 ATP + maltose
-
 Mycolicibacterium smegmatis ADP + maltose 1-phosphate
-
 ?
2.7.1.175 ATP + maltose
-
 Mycolicibacterium smegmatis ATCC 14468 ADP + maltose 1-phosphate
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.99.16 37
-
 assay at Mycolicibacterium smegmatis
2.7.1.175 50
-
-
 Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.99.16 7
-
 assay at Mycolicibacterium smegmatis
2.7.1.175 8.2
-
-
 Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.175 ATP dependent on Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
2.4.99.16 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
2.7.1.175 metabolism the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose Mycolicibacterium smegmatis