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Enzyme Nomenclature
Information on EC 2.4.99.16 - starch synthase (maltosyl-transferring)
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.99.16
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RECOMMENDED NAME
GeneOntology No.
starch synthase (maltosyl-transferring)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n = phosphate + [(1->4)-alpha-D-glucosyl]n+2
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
56093-22-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
metabolism
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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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-deoxy-2-fluoro-alpha-maltosyl fluoride + maltotetraose
?
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?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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-
-
?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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r
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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-
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?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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
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r
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
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?
additional information
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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
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additional information
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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
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additional information
?
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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
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
Q9RP48
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?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
Q9RP48
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?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
Q9L1K2
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?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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maltosaccharides
compete with glycogen for the transferred maltose
additional information
no inhibition by isofagomine or acarbose
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme GMPMT 89fold by ammonium sulfate fractionation, dialysis, anion exchange chromatography and gel filtration
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.99.16)
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