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Information on EC 2.4.99.16 - starch synthase (maltosyl-transferring) and Organism(s) Streptomyces coelicolor and UniProt Accession Q9L1K2

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:
Streptomyces coelicolor
UNIPROT: Q9L1K2
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The taxonomic range for the selected organisms is: Streptomyces coelicolor
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
alpha-maltose 1-phosphate:(1->4)-alpha-D-glucan 4-alpha-D-maltosyltransferase
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maltosyl transferase
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maltosyltransferase GlgE
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alpha1,4-glucan:maltose-1-P maltosyltransferase
-
-
-
-
GMPMT
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
2-deoxy-2-fluoro-alpha-maltosyl fluoride + maltotetraose
?
show the reaction diagram
-
-
-
?
alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl]n
phosphate + [(1->4)-alpha-D-glucosyl]n+2
show the reaction diagram
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug target
the enzyme has been genetically validated as a target for tuberculosis therapies
metabolism
SUBUNIT
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
PROTEIN VARIANTS
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Syson, K.; Stevenson, C.E.; Rashid, A.M.; Saalbach, G.; Tang, M.; Tuukkanen, A.; Svergun, D.I.; Withers, S.G.; Lawson, D.M.; Bornemann, S.
Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds alpha-maltose 1-phosphate and forms a maltosyl-enzyme intermediate
Biochemistry
53
2494-2504
2014
Streptomyces coelicolor (Q9L1K2), Streptomyces coelicolor
Manually annotated by BRENDA team
Rashid, A.M.; Batey, S.F.; Syson, K.; Koliwer-Brandl, H.; Miah, F.; Barclay, J.E.; Findlay, K.C.; Nartowski, K.P.; Khimyak, Y.Z.; Kalscheuer, R.; Bornemann, S.
Assembly of alpha-glucan by GlgE and GlgB in Mycobacteria and Streptomycetes
Biochemistry
55
3270-3284
2016
Mycobacterium tuberculosis (P9WQ17), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WQ17), Streptomyces coelicolor (Q9L1K2), Streptomyces coelicolor ATCC BAA-471 (Q9L1K2)
Manually annotated by BRENDA team
Syson, K.; Stevenson, C.E.; Miah, F.; Barclay, J.E.; Tang, M.; Gorelik, A.; Rashid, A.M.; Lawson, D.M.; Bornemann, S.
Ligand-bound structures and site-directed mutagenesis identify the acceptor and secondary binding sites of Streptomyces coelicolor maltosyltransferase GlgE
J. Biol. Chem.
291
21531-21540
2016
Streptomyces coelicolor (Q9L1K2), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9L1K2)
Manually annotated by BRENDA team