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) Zea mays and UniProt Accession P93805

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:
Zea mays
UNIPROT: P93805
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Zea mays
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
Glucose phosphomutase
-
-
-
-
PGM2
-
-
-
-
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
-
-
r
alpha-D-glucose 1,6-bisphosphate + H2O
alpha-D-glucose 6-phosphate + phosphate
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
D-Mannose 1-phosphate
D-Mannose 6-phosphate
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-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
-
uncompetitive inhibition
AMP
-
-
ATP
-
-
cis-aconitate
-
weak inhibition
citrate
-
-
D-Glucose 1,6-bisphosphate
-
-
D-glucose 1-phosphate
-
-
D-mannose 1-phosphate
-
-
isocitrate
-
weak inhibition
UTP
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose-1,6-bisphosphate
-
6-phosphogluconate
-
-
ADP
-
-
D-fructose-6-phosphate
-
-
D-glucose-1,6-bisphosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
alpha-D-Glucose 1,6-bisphosphate
-
25°C, pH 7.6
0.02
alpha-D-glucose 1-phosphate
-
25°C, pH 7.6
0.02
D-mannose 1-phosphate
-
25°C, pH 7.6
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
D-Glucose 1,6-bisphosphate
-
25°C, pH 7.6, substrate inhibition at high concentrations
3.3
D-glucose 1-phosphate
-
25°C, pH 7.6, substrate inhibition at high concentrations
1.35
D-mannose 1-phosphate
-
25°C, pH 7.6, substrate inhibition at high concentrations
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11.7
-
-
6.53
O2 deprivation for 24 h
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.47
deduced from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGMC2_MAIZE
583
0
63041
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
-
gel filtration
133000
-
gel filtration
63000
x * 63000, deduced from nucleotide sequence
66000
-
2 * 66000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 63000, deduced from nucleotide sequence
dimer
-
2 * 66000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
autophosphorylation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
no loss of activity after 3 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, 50% glycerol, 2-3 d, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Sephadex G-25, DEAE-Toyopearl, Toyopearl HW-65
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Popova, T.N.; Matasova, L.V.; Lapot'ko, A.A.
Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves
Biochem. Mol. Biol. Int.
46
461-470
1998
Zea mays
Manually annotated by BRENDA team
Popova, T.N.; Matasova, L.V.; Lapot'ko, A.A.
Purification and some catalytic properties of phosphoglucomutase from maize leaves
Biochemistry (Moscow)
63
697-701
1998
Zea mays
Manually annotated by BRENDA team
Manjunath, S.; Lee, C.H.; VanWinkle, P.; Bailey-Serres, J.
Molecular and biochemical characterization of cytosolic phosphoglucomutase in maize. Expression during development and in response to oxygen deprivation
Plant Physiol.
117
997-1006
1998
Zea mays (P93804), Zea mays (P93805), Zea mays
Manually annotated by BRENDA team