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Enzyme Nomenclature
Information on EC 2.4.1.342 - alpha-maltose-1-phosphate synthase
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2.4.1.342 alpha-maltose-1-phosphate synthaseIUBMB Comments
The enzyme, found in Mycobacteria, can also use UDP-alpha-D-glucose with much lower catalytic efficiency.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glgA
glgM
glgM
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate = ADP + alpha-maltose-1-phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase (configuration-retaining)
The enzyme, found in Mycobacteria, can also use UDP-alpha-D-glucose with much lower catalytic efficiency.
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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
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate
ADP + alpha-maltose-1-phosphate
-
-
-
?
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate
ADP + alpha-maltose-1-phosphate
-
-
-
?
additional information
?
-
enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity
-
-
-
additional information
?
-
enzyme follows a ternary complex mechanism, whereby ADP-glucose binds to the enzyme before D-glucose 1-phosphate. GlgM shows no detecable glycogen synthase activity
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate
ADP + alpha-maltose-1-phosphate
-
-
-
?
ADP-alpha-D-glucose + alpha-D-glucose-1-phosphate
ADP + alpha-maltose-1-phosphate
-
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.046
ADP-alpha-D-glucose
with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.063
ADP-alpha-D-glucose
with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.121
ADP-alpha-D-glucose
with 1.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.145
ADP-alpha-D-glucose
with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
0.578
alpha-D-glucose-1-phosphate
with 0.5 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
0.695
alpha-D-glucose-1-phosphate
with 4.0 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
0.816
alpha-D-glucose-1-phosphate
with 0.1 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.4
ADP-alpha-D-glucose
with 4.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
19.8
ADP-alpha-D-glucose
with 2.5 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
20
ADP-alpha-D-glucose
with 0.25 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
29.2
ADP-alpha-D-glucose
with 1.0 mM alpha-D-glucose-1-phosphate, at pH 7.0 and 37°C
39
alpha-D-glucose-1-phosphate
with 0.1 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
80.6
alpha-D-glucose-1-phosphate
with 4.0 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
97.9
alpha-D-glucose-1-phosphate
with 0.5 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.578
alpha-D-glucose-1-phosphate
with 0.5 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
0.895
alpha-D-glucose-1-phosphate
with 4.0 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
1.45
alpha-D-glucose-1-phosphate
with 0.1 mM ADP-alpha-D-glucose, at pH 7.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLGM_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
387
0
41679
Swiss-Prot
-
GLGM_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
387
0
41533
Swiss-Prot
-
GLGM_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
387
0
41533
Swiss-Prot
-
A0A645H5U2_9ZZZZ
102
0
11027
TrEMBL
other Location (Reliability: 3)
A0A645FV57_9ZZZZ
237
0
26686
TrEMBL
Mitochondrion (Reliability: 4)
A0A645JPK4_9ZZZZ
109
0
12184
TrEMBL
other Location (Reliability: 2)
A0A6L5BKF5_9PSED
376
0
41784
TrEMBL
-
A0A5A5RNB1_MICAE
356
0
40462
TrEMBL
-
A0A645EZ22_9ZZZZ
244
0
27597
TrEMBL
other Location (Reliability: 1)
A0A564S068_BIFLI
416
0
45527
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure at 1.9 A resolution. GlgM shares a GT-B fold with bacterial glycogen synthases
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koliwer-Brandl, H.; Syson, K.; van de Weerd, R.; Chandra, G.; Appelmelk, B.; Alber, M.; Ioerger, T.; Jacobs, W.J.; Geurtsen, J.; Bornemann, S.; Kalscheuer, R.
Metabolic network for the biosynthesis of intra- and extracellular alpha-glucans required for virulence of Mycobacterium tuberculosis
PLoS Pathog.
12
e1005768
2016
Mycobacterium tuberculosis (P9WMZ1), Mycobacterium tuberculosis H37Rv (P9WMZ1)
brenda
Syson, K.; Stevenson, C.; Lawson, D.; Bornemann, S.
Structure of the Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM
Acta Crystallogr. Sect. F
76
175-181
2020
Mycolicibacterium smegmatis (A0R2E2), Mycolicibacterium smegmatis ATCC 700084 (A0R2E2)
brenda
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