Information on EC 2.4.99.16 - starch synthase (maltosyl-transferring)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.99.16
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RECOMMENDED NAME
GeneOntology No.
starch synthase (maltosyl-transferring)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
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Starch and sucrose metabolism
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-2-fluoro-alpha-maltosyl fluoride + maltotetraose
?
show the reaction diagram
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?
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 SUBSTRATES
NATURAL PRODUCTS
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dideoxy-1,4-imino-D-arabinitol
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2-deoxy-2-fluoro-alpha-maltosyl fluoride
after preincubation for 5 min with 1 mM substrate analogue 2-deoxy-2-fluoro-alpha-maltosyl fluoride, 70% of the normal activity with alpha-maltose 1-phosphate is lost
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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
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-maltose 1-phosphate bound to a D394A mutant and beta-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a E423A mutant is crystallized with 15% (w/v) polyethylene glycol 3350, 0.2 M sodium citrate, and 15% (w/v) ethylene glycol
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme GMPMT 89fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography and gel filtration
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D394A
the maltosyl transferase activity of the mutant is more than 4 orders of magnitude lower than that of the wild type protein
E423A
the mutant turns over alpha-maltose 1-phosphate about 500times slower than the wild type enzyme
Show AA Sequence (2743 entries)
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