Information on EC 5.4.2.8 - phosphomannomutase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
5.4.2.8
-
RECOMMENDED NAME
GeneOntology No.
phosphomannomutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
show the reaction diagram
the cosubstrate glucose-1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
alpha-D-mannose 1-phosphate = D-mannose 6-phosphate
show the reaction diagram
enzyme is activated by transfer of a phosphate group from mannose-1,6-diphosphate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
isomerization
B6Z254, -
-
isomerization
Q9KZL6, -
-
isomerization
-
-
isomerization
-
-
PATHWAY
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
Biosynthesis of secondary metabolites
-
Fructose and mannose metabolism
-
GDP-mannose biosynthesis
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannose 1,6-phosphomutase
alpha-D-Mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha-phosphomannomutase1
Q92871
-
EC 2.7.5.7
-
-
formerly
-
IMP-sensitive glucose-1,6-bisphosphatase
-
-
ORF17
-
-
-
-
PGM/PMM
Sphingobium chungbukense DJ77
-
-
-
PGM2
-
Giardia has two proteins with phosphoglucomutase activity, one of which (PGM2) also has phosphomannomutase activity
phosphomannomutase
O80840
-
phosphomannomutase
-
-
phosphomannomutase
-
-
phosphomannomutase
Q9KZL6
-
phosphomannomutase
B6Z254
-
phosphomannomutase 1
-
-
phosphomannomutase 2
O15305
-
phosphomannomutase/phosphoglucomutase
-
-
Phosphomannose mutase
-
-
-
-
Phosphomutase, mannose
-
-
-
-
PMM
-
-
-
-
PMM
C8C16, C8CK15, C8CK16
-
PMM
C8CK06, C8CK09, C8CK10
-
PMM
-, C8CK11, C8CK12, C8CK13
-
PMM
-
-
PMM-1
-
isoform
PMM-2
O15305
-
PMM-A1
C8CK06
isoform
PMM-A1
C8CK11
isoform
PMM-A1
-
isoform
PMM-B1
C8CK12
isoform
PMM-B2
C8CK13
isoform
PMM-D1
C8CK15
isoform
PMM-D1
C8CK09
isoform
PMM-D2
C8C16, C8CK16
isoform
PMM-D2
C8CK10
isoform
PMM/PGM
-
bifunctinal enzyme
PMM/PGM
-
bifunctional enzyme
PMM/PGM
-
bifunctional enzyme
PMM/PGM
Pyrococcus horikoshii OT-3
-
bifunctional enzyme
-
PMM1
-
multifunctional enzyme
PMMH-22
-
-
-
-
SP-2
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase activities
SP-2
Sphingobium chungbukense DJ77
-
bifunctional enzyme with phosphoglucomutase and phosphomannomutase activities
-
CAS REGISTRY NUMBER
COMMENTARY
59536-73-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform PMM-D1; cultivars AS67 and AS91
UniProt
Manually annotated by BRENDA team
isoform PMM-D2; cultivars AS67 and AS91
C8C16, C8CK16
UniProt
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
cultivar Bd21
-
-
Manually annotated by BRENDA team
Cassia corymbosa
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
human liver enzyme and recombinant PMM1 from individuals with carbohydrate-deficient glycoprotein syndrome type I
-
-
Manually annotated by BRENDA team
isoform alpha-PMM1
SwissProt
Manually annotated by BRENDA team
isoform alpha-PMM2
SwissProt
Manually annotated by BRENDA team
cultivar Betzes
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bifunctional phosphomannomutase/phosphoglucomutase
-
-
Manually annotated by BRENDA team
wild-type strains and alginate-producing strains
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii OT-3
OT3
-
-
Manually annotated by BRENDA team
sec53 cells are deficient in phosphomannomutase
-
-
Manually annotated by BRENDA team
Sphingobium chungbukense DJ77
strain DJ77
-
-
Manually annotated by BRENDA team
isoform PMM-A1; cultivars Xiaoyan 54 and Chinese Spring
UniProt
Manually annotated by BRENDA team
isoform PMM-D1; cultivars Xiaoyan 54 and Chinese Spring
UniProt
Manually annotated by BRENDA team
isoform PMM-D2; cultivars Xiaoyan 54 and Chinese Spring
UniProt
Manually annotated by BRENDA team
cultivar Langdon
-
-
Manually annotated by BRENDA team
isoform PMM-A1; cultivar Langdon
UniProt
Manually annotated by BRENDA team
isoform PMM-B1; cultivar Langdon
UniProt
Manually annotated by BRENDA team
isoform PMM-B2; cultivar Langdon
UniProt
Manually annotated by BRENDA team
cultivars DV877 and IE29-1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
Q92871
alpha-phosphomannomutase1 is required for GDP-mannose and dolichol-phosphate-mannose biosynthesis
physiological function
Q9KZL6, -
phosphomannomutase is important in the direct or/and indirect control of antibiotic production
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-deoxy-D-glucose 6-phosphate
2-deoxy-D-glucose 1-phosphate
show the reaction diagram
-
-
-
-
?
2-deoxyribose 1-phosphate
2-deoxyribose 5-phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-D-glyceric acid
?
show the reaction diagram
-
no mutase activity
-
-
?
alpha-D-glucose 1,6-bisphosphate
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
r
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
P26276
-
-
r
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
Sphingobium chungbukense, Sphingobium chungbukense DJ77
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
P26276
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
C8CK11, C8CK12, C8CK13, -
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
C0JP35, -
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
O15305
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
C8CK06, C8CK09, C8CK10, -
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
C8C16, C8CK15, C8CK16
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
Q92871
the interconversion occurs via a mannose-1,6-(bis) phosphate intermediate
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
Sphingobium chungbukense DJ77
-
preferred substrate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9KZL6, -
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
B6Z254, -
-
-
-
?
alpha-D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-fructose-1-phosphate
D-fructose-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
D-glucosamine-1-phosphate
D-glucosamine-6-phosphate
show the reaction diagram
-
low enzyme activity
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
O15305, Q92871
-
-
-
?
D-glucose 1-phosphate
D-glucose 6-phosphate
show the reaction diagram
O80840
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
O15305, Q92871
-
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
-
bifunctional enzyme
-
-
?
D-glucose-1-phosphate
D-glucose-6-phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
O15305, Q92871
-
-
-
?
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
r
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
r
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
Cassia corymbosa
-
r
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
more slowly in the reverse direction
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate or mannose 1,6-diphosphate
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
-
the cosubstrate glucose-1,6-diphosphate or mannose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
-
-
D-Mannose 1-phosphate
D-Mannose 6-phosphate
show the reaction diagram
O80840
reaction with mannose 1-phosphate is more efficient than with D-glucose-1-phosphate
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
O80840
-
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
-
-
-
r
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
first enzyme of the N-glycosylation pathway
-
-
-
D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
-
bifunctional enzyme
-
-
?
D-mannose-1-phosphate
D-mannose-6-phosphate
show the reaction diagram
Pyrococcus horikoshii OT-3
-
-
-
-
r
D-mannose-1-phosphate
mannose-6-phosphate
show the reaction diagram
-
-
-
-
r
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
N-acetyl-D-glucosamine-1-phosphate
N-acetyl-D-glucosamine-6-phosphate
show the reaction diagram
-
no mutase activity
-
-
?
Glucose 1-phosphate
Glucose 6-phosphate
show the reaction diagram
-
-
-
-
additional information
?
-
-
PMM1 is less specific: it has nearly equal phosphomannomutase and phosphoglucomutase activities as well as a modest glucose-1,6-bisphosphatase activity corresponding to about 3% of its phosphomannomutase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate
alpha-D-glucose 6-phosphate
show the reaction diagram
P26276
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
-
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
20fold higher activity than with alpha-D-glucose 1-phosphate
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
PMM/PGM catalyzes the second step in alginate biosynthesis
-
r
alpha-D-mannose 1-phosphate
alpha-D-mannose 6-phosphate
show the reaction diagram
-
second step of the alginate biosynthetic pathway
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
-
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q9KZL6, -
-
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
B6Z254, -
-
-
-
?
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
the enzyme produces mannose 1-phosphate for the synthesis of mannose-1,6-diphosphate as well as of GDPmannose
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
the enzyme is required for synthesis of lipopolysaccharide O side chains
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
conversion to mannose 1-phosphate, which is a substrate for the synthesis of GDPmannose. This nucleotide sugar is then used in the synthesis of dolichol-phosphate-mannose, which is essential for N-linked glycosylation and thus the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol anchored proteins
-
-
-
D-mannose 6-phosphate
D-mannose 1-phosphate
show the reaction diagram
-
first enzyme of the N-glycosylation pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1% relative activity
Co2+
-
72% of the activation relative to Mg2+, maximal activity at 0.5 mM
Co2+
-
divalent cation required, at 2.0 mM 57% of the activation relative to Mg2+
Co2+
-
44% relative activity
Mg2+
Cassia corymbosa
-
maximal activation at 2.5 mM; required
Mg2+
-
maximal activity at 1 mM; required
Mg2+
-
divalent cation required, Mg2+ is most effective; maximal activation at 2.0 mM
Mg2+
-
approx. 3fold activation at 1 mM-5 mM
Mg2+
-
required for activity
Mg2+
-
100% relative activity
Mg2+
-
highest activity in the presence of Mg2+
Mn2+
-
divalent cation required, at 2.0 mM 7% of the activation relative to Mg2+
Ni2+
-
36% of the activation relative to Mg2+, maximal activity at 0.5 mM
Ni2+
-
divalent cation required, at 2.0 mM 22% of the activation relative to Mg2+
Ni2+
-
15% relative activity
Mn2+
-
20% relative activity
additional information
-
Ni2+, Mn2+ and Zn2+ at a concentration of 1 mM can also support activity, although to a lesser extent
additional information
-
no detectable activity after addition of 0.1 mM EDTA
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-deoxyglucose 6-phosphate
-
-
Be2+
-
in histidine buffer
Cu2+
-
in Tris buffer, no inhibition in histidine buffer
Disperse Blue 56
-
kinetic studies indicate that it is a parabolic, noncompetitive inhibitor. Reduction of the inhibition in the presence of 0.01% Triton X-100
fructose 1-phosphate
-
-
glucose 1-phosphate
-
substrate inhibition of reverse reaction
glucose 6-phosphate
-
poor, competitive with respect to mannose 6-phosphate
IMP
-
IMP stimulates by more than 100fold the intrinsic glucose-1,6-bisphosphatase activity of recombinant PMM1 while inhibiting its phosphoglucomutase activity
mannose 1-phosphate
-
at high concentrations, competitive with respect to glucose-1,6-diphosphate, Ki: 1.2 mM
mannose 1-phosphate
-
above 0.15 mM
serum- and glucocorticoid-regulated kinase
-
Sgk1 decreases the enzymatic activity of PMM2 in the basal state and upon insulin stimulation in intact COS-7 cells
-
vanadate
-
0.05 mM, 50% inhibition
Zn2+
-
in Tris buffer, no inhibition in histidine buffer
Mn2+
-
complete inhibition above 2 mM
additional information
-
not inhibitory: 1,5-diamino-4,8-dihydroxyanthraquinone
-
additional information
Q9KZL6, -
a deletion mutant is constructed
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
alpha-D-glucose 1,6-diphosphate
Cassia corymbosa
-
Km: 0.00087 mM; or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.16 mM; or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.0003 mM; or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
Km: 0.15 mM; required
alpha-D-glucose 1,6-diphosphate
-
or alpha-D-mannose 1,6-diphosphate required
alpha-D-glucose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-glucose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from glucose 1,6-diphosphate
alpha-D-Mannose 1,6-diphosphate
Cassia corymbosa
-
Km: 0.0025 mM; or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
Km: 0.12 mM; or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
Km: 0.0003 mM; or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
or alpha-D-glucose 1,6-diphosphate required
alpha-D-Mannose 1,6-diphosphate
-
the cosubstrate glucose 1,6-diphosphate is converted to the corresponding sugar monophosphate while the substrate is converted to the sugar biphosphate in each reaction cycle
alpha-D-Mannose 1,6-diphosphate
-
enzyme is activated by transfer of a phosphate group from mannose 1,6-diphosphate
D-Glucose 1,6-bisphosphate
-
-
D-Glucose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as mannose 1,6-bisphosphate in activation
D-Glucose 1,6-bisphosphate
O80840
in presence of 0.02 and 0.2 mM mannose 1-phosphate substrate, half-maximal stimulation of recombinant enzyme at 0.004 and 0.008 mM D-glucose 1,6-bisphosphate
D-Glucose 1,6-bisphosphate
C0JP35, -
required for activity
D-Mannose 1,6-bisphosphate
-
PMM2 requires a hexose bisphosphate for activity, as potent as glucose 1,6-bisphosphate in activation, half-maximal activation in the presence of 0.01 mM and 0.1 mM at 0.0005 mM and 0.001 mM mannose 1,6-bisphosphate, respectively
histidine
Cassia corymbosa
-
required, maximal activation at 10 mM
Insulin
-
incubation with insulin for 45min led to a more than twofold activation of the enzyme
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.5
-
2-deoxyribose-1-phosphate
-
90C
0.0127
-
alpha-D-glucose 1-phosphate
-
mutant RN110A
0.0132
-
alpha-D-glucose 1-phosphate
-
mutant R15A
0.0195
-
alpha-D-glucose 1-phosphate
-
mutant R247A
0.0272
-
alpha-D-glucose 1-phosphate
-
wild type enzyme, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0273
-
alpha-D-glucose 1-phosphate
-
wild-type
0.0279
-
alpha-D-glucose 1-phosphate
-
mutant R421C
0.0354
-
alpha-D-glucose 1-phosphate
-
mutant enzyme P368A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0366
-
alpha-D-glucose 1-phosphate
-
mutant enzyme S369A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0489
-
alpha-D-glucose 1-phosphate
-
mutant enzyme P368G, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0491
-
alpha-D-glucose 1-phosphate
-
mutant enzyme R262A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0493
-
alpha-D-glucose 1-phosphate
-
mutant enzyme Y17A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0518
-
alpha-D-glucose 1-phosphate
-
mutant enzyme E325A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.0667
-
alpha-D-glucose 1-phosphate
-
mutant enzyme R262A/P368G, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.4516
-
alpha-D-glucose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37C
0.0056
-
alpha-D-mannose 1-phosphate
-
in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
0.068
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 28C
0.111
-
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 28C
0.1569
-
alpha-D-mannose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37C
0.2
-
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 28C
0.204
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 18C
0.229
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 28C
0.294
-
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 18C
0.387
-
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 18C
0.4
-
alpha-D-mannose 1-phosphate
C8CK06, C8CK09, C8CK10, -
isoform PMM-D1, 30C, pH not specified in the publication
0.46
-
alpha-D-mannose 1-phosphate
C8CK06, C8CK09, C8CK10, -
isoform PMM-A1, 37C, pH not specified in the publication
0.475
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 18C
0.48
-
alpha-D-mannose 1-phosphate
C8CK06, C8CK09, C8CK10, -
isoform PMM-D2, 30C, pH not specified in the publication
0.0075
-
D-glucose 1-phosphate
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
0.012
-
D-glucose 1-phosphate
-
-
0.0654
-
D-glucose 1-phosphate
O80840
30C, pH 7.5
0.0135
-
D-glucose-1-phosphate
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
0.0952
-
D-glucose-1-phosphate
-
isoenzyme PH0923, 65C
0.127
-
D-glucose-1-phosphate
-
isoenzyme PH0923S101A, 65C
3
-
D-glucose-1-phosphate
-
90C
0.018
-
D-mannose 1-phosphate
-
-
0.0297
-
D-mannose 1-phosphate
O80840
30C, pH 7.5
0.054
-
D-mannose 1-phosphate
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
0.15
-
D-mannose 1-phosphate
Cassia corymbosa
-
-
1.37
-
D-mannose 1-phosphate
-
-
0.3
0.5
D-mannose 6-phosphate
Cassia corymbosa
-
-
0.016
-
D-mannose-1-phosphate
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
0.0915
-
D-mannose-1-phosphate
-
isoenzyme PH0923, 37C
3.2
-
D-mannose-1-phosphate
-
90C
0.0013
-
glucose 1-phosphate
-
H308N/H329N double mutant; S108A mutant
0.0024
-
glucose 1-phosphate
-
S108A/H308N double mutant
0.0027
-
glucose 1-phosphate
-
K118L/H109Q double mutant
0.0028
-
glucose 1-phosphate
-
R20A mutant
0.0034
-
glucose 1-phosphate
-
S108D mutant
0.006
-
glucose 1-phosphate
-
recombinant enzyme PMM1
0.008
-
glucose 1-phosphate
-
H109Q mutant; K118L mutant
0.009
-
glucose 1-phosphate
-
R247A mutant
0.01
-
glucose 1-phosphate
-
H308N mutant; S108V mutant
0.012
-
glucose 1-phosphate
-
-
0.016
-
glucose 1-phosphate
-
H329N mutant
0.022
-
glucose 1-phosphate
-
-
0.003
-
mannose 1-phosphate
-
-
0.0032
-
mannose 1-phosphate
-
recombinant enzyme PMM1
0.016
-
mannose 1-phosphate
-
in presence of glucose 1,6-diphosphate
0.06
-
mannose 1-phosphate
-
-
0.2
-
mannose 1-phosphate
-
-
0.074
-
mannose 6-phosphate
-
in presence of glucose 1,6-diphosphate
additional information
-
additional information
-
KM mannose-1-phosphate isoenzyme PH0923S101A not detectable, 37C
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.012
-
alpha-D-glucose 1-phosphate
-
mutant enzyme E325A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.05
-
alpha-D-glucose 1-phosphate
-
mutant enzyme Y17A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.48
-
alpha-D-glucose 1-phosphate
-
mutant enzyme R262A/P368G, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
0.87
-
alpha-D-glucose 1-phosphate
-
mutant enzyme R262A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.02
-
alpha-D-glucose 1-phosphate
-
mutant enzyme P368A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
1.23
-
alpha-D-glucose 1-phosphate
-
mutant enzyme P368G, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
2.17
-
alpha-D-glucose 1-phosphate
-
mutant enzyme S369A, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
7.83
-
alpha-D-glucose 1-phosphate
-
wild type enzyme, at 25C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4
82.93
-
alpha-D-glucose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37C
0.18
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 18C
0.24
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R/R37Q, at 28C
0.44
-
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 18C
0.67
-
alpha-D-mannose 1-phosphate
-
mutant enzyme R37Q, at 28C
4.13
-
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 18C
4.18
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 18C
10.01
-
alpha-D-mannose 1-phosphate
-
wild type enzyme, at 28C
10.31
-
alpha-D-mannose 1-phosphate
-
mutant enzyme G7R, at 28C
134.9
-
alpha-D-mannose 1-phosphate
-
in 50 mM Tris-HCl (pH 7.5), at 37C
2.85
-
D-glucose 1-phosphate
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
1.72
-
D-glucose-1-phosphate
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
4.4
-
D-mannose 1-phosphate
O15305, Q92871
isoform alpha-PMM1, pH 6.5, 25C
3.9
-
D-mannose-1-phosphate
O15305, Q92871
isoform alpha-PMM2, pH 6.5, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
using alpha-D-mannose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
49
-
-
-
additional information
-
-
2-deoxyribose-1-phosphate Vmax 0.230, 90C; D-glucose-1-phosphate Vmax 0.690, 90C, pH 7.0; D-mannose-1-phosphate Vmax 0.401, 90C
additional information
-
-
isoenzyme PH0923 PGM Vmax 24, 65C; isoenzyme PH0923 PMM Vmax 0.7, 37C; isoenzyme PH0923S101A PGM Vmax 0.4, 65C; isoenzyme PH0923S101A PMM Vmax not detectable, 37C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7
Cassia corymbosa
-
-
6.5
-
-
-
7
-
-
10mM Mg2+, 90C
7.1
-
O80840
95% of maximum activity
7.4
-
-
-
7.5
-
O80840
-
7.5
-
Q9KZL6, -
activity assay
7.5
-
-
activity assay
7.8
-
-
kinetic assay
9
-
-
around, bicine-NaOH buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.6
Cassia corymbosa
-
50% of maximal activity at pH 5.5 and at pH 7.6
7.1
-
-
80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
kinetic assay
30
-
Q9KZL6, -
activity assay
30
-
C8CK06, C8CK09, C8CK10, -
isoform PMM-D1; isoform PMM-D2
37
-
-
activity assay
37
-
C8CK06, C8CK09, C8CK10, -
isoform PMM-A1
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
37
-
-
30
37
-
the enzyme activity level is reduced by nearly 95% as the temperature increases from 30 to 37C
30
37
-
the isoform PMM-1 activity level decreases sharply (by more than 90%) as the temperature shifts from 30 to 37C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.12
-
C0JP35, -
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Cassia corymbosa
-
developing
Manually annotated by BRENDA team
additional information
O80840
enzyme is constitutively expressed in both vegetative and reproductive organs
Manually annotated by BRENDA team
additional information
-
enzyme is constitutively expressed in both vegetative and reproductive organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
expression in COS-7 cells
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27900
-
C0JP35, -
calculated from amino acid sequence
29000
-
-
immunoprecipitation using 9e10 antibody
38000
-
-
gel filtration
41000
-
Cassia corymbosa
-
density gradient ultracentrifugation
50000
-
-
SDS-PAGE
55000
-
-
gel filtration
58000
-
Cassia corymbosa
-
gel filtration
60000
-
-
gel filtration
62000
-
-
gel filtration
105400
-
-
native enzyme, non-denaturing PAGE
210000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 31100, SDS-PAGE
?
Q95ZD7
x * 31100, SDS-PAGE
?
O80840
x * 27700, calculated and MALDI-TOF
dimer
-
2 * 29000
dimer
-
2 * 30000, SDS-PAGE
homodimer
-
2 * 51000, SDS-PAGE
homodimer
Sphingobium chungbukense DJ77
-
2 * 51000, SDS-PAGE
-
tetramer
-
4 * 49850, protein encoded by gene TK1108, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue, so that activity is reduced only 20fold from that of wild-type
phosphoprotein
-
active form of PMM/PGM is phosphorylated at Ser108
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isoform alpha-PMM1 in the open conformation, with and without bound substrate alpha-D-mannose 1-phosphate. Protein consists of two domains, the cap and the core. Substrate phosphate group is at a positively charged site of the cap domain, suggesting that substrate binds first to the cap and then is swept into the active site, thereby facilitating its closure over the core domain
O15305, Q92871
free enzyme and in complex with glucose 1,6-bisphosphate at 2.1 and 2.9 A resolution, resp. Comparison with structure of human enzyme
-, Q95ZD7
12-15 mg/ml PMM/PGM solution in 10 mM MOPS, crystals grow by hanging-drop vapor diffusion from 1.4 M sodium/potassium tartrate and 100 mM Na-HEPES, pH 7.5 from drops containing 0.002 ml protein and 0.002 ml of well buffer, crystals diffract to 1.75 A
-
crystal structure of the selenomethionine-substituted PMM/PGM at 2.2 A resolution, crystal structure of S108A mutant at 1.75 A resolution
-
in complex with inhibitor xylose 1-phosphate or slow substrate ribose 1-phosphate. Both ligands induce an interdomain rearrangement, using different enzyme-ligand interactions
-
mutant enzyme P368G, hanging drop vapour diffusion method
-
phospho- and dephospho-enzyme in complex with reaction intermediate glucose 1,6-bisphosphate at 1.9 and 2.0 A
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
maximal stability
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
38
-
-
50% loss of activity within a few min, completely protected from heat inactivation by 1 mM mannose 1-phosphate, 0.01 mM glucose 1,6-diphosphate or 1 mM fructose 1,6-diphosphate. In presence of 1 mM Mg2+: 50% loss of activity after 17 min
50
-
-
40% loss of activity after 3 min
95
-
-
longer than 90 min stable
100
-
-
highly stable, half-life of about 85 min in boiling water in presence of 10mM Mg2+
100
-
-
50% activity after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Mg2+ stabilizes
-
higly unstable during storage
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 2 months
-
0-4C, 50% glycerol, 12 h, 70% loss of activity
-
0-4C, 50% glycerol, 3-4 d, complete loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Talon metal affinity resin chromatography
-
nickel affinity chromatography column chromatography
-
-
Cassia corymbosa
-
cell extracts are purified by His-tag agarose beads
-
Ni-Sepharose column chromatography
-
recombinant PMM2, polyethylene glycol, DEAE-Sepharose, Q-Sepharose
-
nickel affinity chromatography column chromatography
-
Ni-NTA column chromatography
-
partial, alginate-producing strain V388
-
recombinant PGM
-
recombinant PMM/PGM
-
nickel-affinity column chromatography
-
nickel-chelating resin chromatography
-
heat treatment 85C, 20 min, anion-exchange, hydrophobic and gel filtration column chromatography
-
nickel affinity chromatography column chromatography; nickel affinity chromatography column chromatography; nickel affinity chromatography column chromatography
C8CK06, C8CK09, C8CK10, -
ammonium sulfate, Sephadex G-25, KM-cellulose, partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain BL21(DE3)pLysE cells
-
expression in Agrobacterium tumefaciens
O80840
expression in Escherichia coli with His-tag, expression as green fluorescent protein fusion protein in Arabidospsis thaliana
O80840
expressed in Escherichia coli
-
into the vector pET24ma for transformation of Escherichia coli BL21DE3 cells
-
expressed in Saccharomyces cerevisiae strain BY4741
-
expressed in Escherichia coli BL21 cells
O15305
expression in a temperature-sensitive mutant sec53 yeast strain, expression in BHK cells
-
expression in Escherichia coli
-
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
-
expressed in Escherichia coli
-
expression in Escherichia coli
-, Q95ZD7
expressed in Nicotiana tabacum
C0JP35, -
expressed in Escherichia coli BL21(DE3) cells and HEK-293T cells
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
nucleotide sequence of wild-type and mutant algC genes as well as the transcription and translational initiation sites of the wild-type gene
-
overexpression in Escherichia coli
-
expression in Escherichia coli
-
overexpression in Escherichia coli BL21
-
expressed in Escherichia coli BL21(DE3) cells
-
the vectors pET24ma, pIBR25 and pKC1139 are used
Q9KZL6, -
expression in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
C8CK06, C8CK09, C8CK10, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
G7R
-
mutant exhibits activity similar to wild type enzyme
R37Q
-
mutant exhibits decreased activity similar to wild type enzyme
C241S
O15305
the mutant shows 60% residual activity the mutation is associated with phosphomannomutase 2 deficiency
D188G |
O15305, Q92871
mutant of isoform PMM2, 2% of wild-type activiy, involved in congential disorder of glycosylation type 1a
D209G
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
D65Y
O15305, Q92871
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
D65Y
O15305
the mutant shows 20% residual activity the mutation is associated with phosphomannomutase 2 deficiency
E197A
O15305
the mutant has wild type activity
F119L
O15305, Q92871
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
F157S
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
F207S
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
P113L
O15305
the mutant shows 43% residual activity, the mutation is associated with phosphomannomutase 2 deficiency
P184T
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R123Q
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R141H
O15305, Q92871
mutant of isoform PMM2, 0.4% of wild-type activiy, involved in congential disorder of glycosylation type 1a
R141H
O15305
inactive, the mutation is associated with phosphomannomutase 2 deficiency
R162W
O15305, Q92871
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
T118S
O15305
the mutant shows 1% residual activity the mutation is associated with phosphomannomutase 2 deficiency
T237M
O15305
the mutant shows 48% residual activity the mutation is associated with phosphomannomutase 2 deficiency
V129M
O15305, Q92871
mutant of isoform PMM2, involved in congential disorder of glycosylation type 1a
V231M
O15305, Q92871
mutant of isoform PMM2, loss of stability at 40C, involved in congential disorder of glycosylation type 1a
E325A
-
mutant shows 0.08% of wild type activity
H109Q
-
6% of wild-type activity
H308N
-
100% of wild-type activity
H308N/H329N
-
5% of wild-type activity
H329N
-
6% of wild-type activity
K118L
-
4% of wild-type activity
K118L/H109Q
-
5% of wild-type activity
N110A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
P368A
-
mutant shows 10% of wild type activity
P368G
-
mutant shows 8.7% of wild type activity
R15A
-
no remarkable differences in Km and Vmax value compared to wild-type, but intermediate glucose-1,6-bisphosphate dissociates from mutant 25times more often than from wild-type
R20A
-
12% of wild-type activity
R20A
-
no catalytic activity
R241C
-
0.3% of wild-type acivity, with Km value similar to wild-type
R247A
-
9% of wild-type activity
R247A
-
no remarkable differences in Km and Vmax value compared to wild-type, modest increase in dissociation of intermediate glucose-1,6-bisphosphate from enzyme
R262A
-
mutant shows 6.1% of wild type activity
R262A/P368G
-
mutant shows 2.5% of wild type activity
S108
-
crystal structure, 5% of wild-type activity
S108A
-
12% of wild-type activity
S108A/H109Q
-
6% of wild-type activity
S108A/H308N
-
3% of wild-type activity
S108A/H329N
-
no activity
S108D
-
7% of wild-type activity
S108V
-
1% of wild-type activity
S10V
-
5% of wild-type activity
S369A
-
mutant shows 20.5% of wild type activity
Y17A
-
mutant shows 0.35% of wild type activity
S101A
-
mutant protein PH0923S101A to investigate the role of the serine residue
S101A
Pyrococcus horikoshii OT-3
-
mutant protein PH0923S101A to investigate the role of the serine residue
-
DELTAmanAB
B6Z254, -
phosphomannose isomerase, phosphomannosemutase double mutant
G7R/R37Q
-
temperature-sensitive Arabidopsis thaliana PMM-12 mutant (G7R/R37Q) has lower PMM protein and enzyme activity levels than the wild type enzyme
additional information
O80840
expression as green fluorescent protein fusion protein in Arabidospsis thaliana increases ascorbic acid content by 25-33%
L32R
O15305
the mutant shows 45% residual activity the mutation is associated with phosphomannomutase 2 deficiency
additional information
-
expression in Leishmania mexicana does not restore virulence of an enzyme deletion mutant
V44A
O15305
the mutant shows 16% residual activity the mutation is associated with phosphomannomutase 2 deficiency
additional information
-, Q95ZD7
enzyme knock-out mutant is avirulent
additional information
-
reducing enzyme expression level through virus-induced gene silencing causes substantial decrease in ascorbic acid content in leaves. Raising the expression level leads to 20-50% increase in ascorbic acid content
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
biotechnology
-
enzymatic synthesis of TMP and 2-deoxy-6-phosphate glucose can successfully produce large amount of TDP-2-deoxy-glucose in one-pot by employing phosphomannomutase
medicine
O15305, Q92871
analysis of clinically important mutations involved in congential disorder of glycosylation type 1a; analysis of clinically important mutations involved in congential disorder of glycosylation type 1a
biotechnology
B6Z254, -
the double mutant lacking the PMI and PMM genes produces 8-deoxyamphoteronolides in good yields along with trace levels of glycosylated amphotericins, with further genetic engineering these mutants may activate alternative hexoses as GDP-sugars for transfer to aglycones in vivo