Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.4.2.2 - phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC5.4.2.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucomutase, phosphoglucomutase 1, phosphomannomutase/phosphoglucomutase, pmm/pgm, alpha-phosphoglucomutase, pgm/pmm, alpha-pgm, phosphoglucose mutase, phosphoglucomutase1, plastidic phosphoglucomutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-Pgm
-
alpha-phosphoglucomutase 1
-
Glucose phosphomutase
-
-
-
-
PGM
-
-
-
-
PGM2
-
-
-
-
phosphoglucomutase 1
-
phosphoglucomutase1
-
Phosphoglucose mutase
-
-
-
-
Phosphomutase, glucose
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose 1,6-phosphomutase
Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. The enzyme also catalyses (more slowly) the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. cf. EC 5.4.2.5, phosphoglucomutase (glucose-cofactor).
CAS REGISTRY NUMBER
COMMENTARY hide
9001-81-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
additional information
?
-
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-D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-bisphosphoglycerate
-
-
fructose 1,6-diphosphate
-
-
additional information
enzyme with a C-terminus 6xHis tag completely loses activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-D-Glucose 1,6-bisphosphate
alpha-D-glucose 1,6-diphosphate
-
Km: 0.00077-0.00163 mM
cysteine
-
required
GSH
-
required
histidine
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057 - 0.088
alpha-D-glucose 1-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1263
-
isozyme PGM1, substrate glucose 1-phosphate
1442
-
isozyme PGM1, substrate glucose 1-phosphate
40.2
-
isozyme PGM2, substrate glucose 1-phosphate
42
-
isozyme PGM2, substrate glucose 1-phosphate
additional information
-
assay method for serum
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.6
-
-
8
-
isozymes PGM1 and PGM2
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme depletion is associated with declined cellular glycogen content and decreased rates of glycogenolysis and glycogenesis. Furthermore, enzyme depletion suppresses cell proliferation under long-term repetitive glucose depletion
physiological function
the enzyme is necessary for sustained cell growth under repetitive glucose depletion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGM1_HUMAN
562
0
61449
Swiss-Prot
other Location (Reliability: 4)
PGM2_HUMAN
612
0
68283
Swiss-Prot
other Location (Reliability: 1)
Q9H1D2_HUMAN
153
0
16270
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58500
-
isozyme PGM1, gel filtration, SDS-PAGE
69000
-
isozyme PGM2, gel filtration, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 65000, calculated from amino acid sequence
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, mutant enzyme D263Y crystals grow in solutions including lithium or ammonium sulfate (1.4-1.55 M) with 0.1 M buffer of either MES, pH 6.0, or Tris HCl, pH 7.5. Crystals of mutant enzyme D263G grow from 1.6 M ammonium sulfate, 0.1 M NaCl, and 0.1 M HEPES, pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A139T
disease-associated missense variant
D263G
D263Y
D288G
disease-associated missense variant
D62H
disease-associated missense variant
E377K
disease-associated missense variant
E388K
disease-associated missense variant
G121R
disease-associated missense variant
G121W
disease-associated missense variant
G230E
disease-associated missense variant
G291R
disease-associated missense variant
G330R
disease-associated missense variant
G375V
disease-associated missense variant
G380R
disease-associated missense variant
G506S
disease-associated missense variant
G508R
disease-associated missense variant
G511R
disease-associated missense variant
H261D
disease-associated missense variant
L516P
disease-associated missense variant
N38Y
disease-associated missense variant
P336R
disease-associated missense variant
Q41E
disease-associated missense variant
Q41H
disease-associated missense variant
Q41R
disease-associated missense variant
R422Q
disease-associated missense variant
R422W
disease-associated missense variant
R503Q
disease-associated missense variant
R515L
disease-associated missense variant
R515Q
disease-associated missense variant
R515W
disease-associated missense variant
S505R
disease-associated missense variant
T115A
disease-associated missense variant
T19A
disease-associated missense variant
T337M
disease-associated missense variant
T556A
the mutant shows about wild type activity
T556E
the mutant shows about wild type activity
T559A
the mutant shows about wild type activity
T559E
the mutant shows about wild type activity
T562A
the mutant shows slightly reduced activity compared to the wild type enzyme
T562E
the mutant shows strongly reduced activity compared to the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes PGM1 and PGM2
-
Ni-NTA agarose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 and Rosetta(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
inhibition of phosphoglucomutase activity by chronic treatment with Li+ causes compensatory elevation of phosphoglucomutase activity in Li+-treated bipolar patients due to increased expression of PGM1 gene
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fazi, A.; Piacentini, M.P.; Piatti, E.; Accorsi, A.
Purification and partial characterization of the phosphoglucomutase isozymes from human placenta
Prep. Biochem.
20
219-240
1990
Homo sapiens
Manually annotated by BRENDA team
Accorsi, A.; Piatti, E.; Piacentini, M.P.; Gini, S.; Fazi, A.
Isoenzymes of phosphoglucomutase from human blood cells: isolation and kinetic properties
Prep. Biochem.
19
251-271
1989
Homo sapiens
Manually annotated by BRENDA team
King, J.
Phosphoglucomutase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
1
826-829
1974
Homo sapiens
-
Manually annotated by BRENDA team
Csutora, P.; Karsai, A.; Nagy, T.; Vas, B.; Kovacs, G.L.; Rideg, O.; Bogner, P.; Miseta, A.
Lithium induces phosphoglucomutase activity in various tissues of rats and in bipolar patients
Int. J. Neuropsychopharmacol.
9
613-619
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Bras, N.F.; Fernandes, P.A.; Ramos, M.J.; Schwartz, S.D.
Mechanistic insights on human phosphoglucomutase revealed by transition path sampling and molecular dynamics calculations
Chemistry
24
1978-1987
2018
Homo sapiens (P36871), Homo sapiens
Manually annotated by BRENDA team
Stiers, K.M.; Graham, A.C.; Kain, B.N.; Beamer, L.J.
Asp263 missense variants perturb the active site of human phosphoglucomutase 1
FEBS J.
284
937-947
2017
Homo sapiens (P36871), Homo sapiens
Manually annotated by BRENDA team
Bae, E.; Kim, H.E.; Koh, E.; Kim, K.S.
Phosphoglucomutase1 is necessary for sustained cell growth under repetitive glucose depletion
FEBS Lett.
588
3074-3080
2014
Homo sapiens (P36871)
Manually annotated by BRENDA team
Muenks, A.G.; Stiers, K.M.; Beamer, L.J.
Sequence-structure relationships, expression profiles, and disease-associated mutations in the paralogs of phosphoglucomutase 1
PLoS ONE
12
e0183563
2017
Homo sapiens (P36871), Homo sapiens
Manually annotated by BRENDA team