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Information on EC 2.4.99.16 - starch synthase (maltosyl-transferring) and Organism(s) Mycolicibacterium smegmatis and UniProt Accession Q9RP48

for references in articles please use BRENDA:EC2.4.99.16
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EC Tree
IUBMB Comments
The enzyme from the bacterium Mycobacterium smegmatis is specific for maltose. It has no activity with alpha-D-glucose.
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This record set is specific for:
Mycolicibacterium smegmatis
UNIPROT: Q9RP48
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The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
maltosyl transferase, gmpmt, maltosyltransferase glge, glge isoform i, alpha1,4-glucan:maltose-1-p maltosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha1,4-glucan:maltose-1-P maltosyltransferase
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alpha1,4-glucan:maltose-1-P maltosyltransferase
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GMPMT
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase
The enzyme from the bacterium Mycobacterium smegmatis is specific for maltose. It has no activity with alpha-D-glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
56093-22-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
show the reaction diagram
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dideoxy-1,4-imino-D-arabinitol
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ATP
strong inhibition
D-glucose 1-phosphate
slight inhibition
D-glucose 6-phosphate
slight inhibition
diphosphate
slight inhibition
maltosaccharides
compete with glycogen for the transferred maltose
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.76
purified enzyme, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme GMPMT 89fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography and gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Biol. Chem.
285
9803-9812
2010
Mycolicibacterium smegmatis (Q9RP48), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 14468 (Q9RP48)
Manually annotated by BRENDA team