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
LITERATURE
alpha-D-glucose 1-phosphate = D-glucose 6-phosphate
show the reaction diagram
acid-base catalysis mechanism, key role for conformational change in its multistep reaction, which requires a dramatic 180 degree reorientation of the intermediate within the active site. Modeling shows that increased enzyme flexibility facilitates the reorientation of the reaction intermediate, coupling changes in structural dynamics with the unique catalytic mechanism of this enzyme
-
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
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
isomerization
-
-
isomerization
-
-
isomerization
Q9KZL6
-
isomerization
B6Z254
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
beta-1,4-D-mannosyl-N-acetyl-D-glucosamine degradation
-
-
Biosynthesis of secondary metabolites
-
-
d-mannose degradation
-
-
Fructose and mannose metabolism
-
-
GDP-mannose biosynthesis
-
-
L-ascorbate biosynthesis I (L-galactose pathway)
-
-
mannan degradation
-
-
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
COMMENTARY
LITERATURE
alpha-phosphomannomutase1
Q92871
-
EC 2.7.5.7
-
-
formerly
-
IMP-sensitive glucose-1,6-bisphosphatase
-
-
ORF17
-
-
-
-
PGM/PMM
Sphingobium chungbukense DJ77
-
-
-
PGM/PMM
Sphingomonas sanxanigenens NX02
M1T754
-
-
PGM2
-
Giardia has two proteins with phosphoglucomutase activity, one of which (PGM2) also has phosphomannomutase activity
PgmG
M1T754
gene name
phosphoglucomutase/phosphomannomutase
M1T754
-
phosphoglucomutase/phosphomannomutase
Sphingomonas sanxanigenens NX02
M1T754
-
-
Phosphohexomutase
Q980S1
-
Phosphohexomutase
Q980S1
-
-
phosphomannomutase
O80840
-
phosphomannomutase
-
-
phosphomannomutase
-
-
phosphomannomutase
Q9KZL6
-
phosphomannomutase
B6Z254
-
phosphomannomutase 1
-
-
phosphomannomutase 2
O15305
-
phosphomannomutase/phosphoglucomutase
-
-
Phosphomannose mutase
-
-
-
-
Phosphomutase, mannose
-
-
-
-
PMM
-
-
-
-
PMM
C8CK15, C8CK16
-
PMM
C8CK06, C8CK09, C8CK10
-
PMM
C8CK11, C8CK12, C8CK13
-
PMM
F4NCC2
gene name
PMM
Trypanosoma brucei 427
F4NCC2
gene name
-
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
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
-
SSO0207
Q980S1
locus name
SSO0207
Q980S1
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
59536-73-1
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PMM-D1; cultivars AS67 and AS91
UniProt
Manually annotated by BRENDA team
isoform PMM-D2; cultivars AS67 and AS91
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
Sphingomonas sanxanigenens NX02
gene pgmG
UniProt
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
gene PMM
UniProt
Manually annotated by BRENDA team
Trypanosoma brucei 427
gene PMM
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
F4NCC2
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
evolution
Trypanosoma brucei 427
-
the enzyme belongs to the alpha-D-phosphohexomutase superfamily of enzymes
-
physiological function
Q9KZL6
phosphomannomutase is important in the direct or/and indirect control of antibiotic production
physiological function
-
the enzyme catalyzes an intramolecular phosphoryl transfer across its phosphosugar substrates, which are precursors in the synthesis of exoproducts involved in bacterial virulence
physiological function
F4NCC2
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphoacetylglucosamine mutase, EC 5.4.2.3, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
physiological function
M1T754
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
physiological function
Trypanosoma brucei 427
-
the enzyme is essential for parasite growth. It takes over the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphoacetylglucosamine mutase, EC 5.4.2.3, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
physiological function
Sphingomonas sanxanigenens NX02
-
the enzyme is involved in biosynthesis of sphingans, extracellular polysaccharides
-
metabolism
Q92871
alpha-phosphomannomutase1 is required for GDP-mannose and dolichol-phosphate-mannose biosynthesis
additional information
-
analysis of conformational flexibility of different forms of phosphoglucomutase/phosphomannomutase in solution, including its active, phosphorylated state and the unphosphorylated state that occurs transiently during the catalytic cycle, by hydrogen-deuterium exchange by mass spectrometry and small angle x-ray scattering. Both ligand binding and phosphorylation of the catalytic phosphoserine affect the overall flexibility of the enzyme in solution
additional information
F4NCC2
the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains
additional information
Trypanosoma brucei 427
-
the cap domain contributes the residues involved in substrate recognition, E119, R121, M124, N126, R132, R139, S177, so that the active site is located in the groove at the interface of the core and cap domains
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
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
M1T754
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
F4NCC2
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q980S1
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Trypanosoma brucei 427
F4NCC2
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Sphingomonas sanxanigenens NX02
M1T754
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
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 6-phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
D-mannose 6-phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
Q980S1
the enzyme also catalyzes the interconversion of alpha-D-glucose 1-phosphate to D-glucose 6-phosphate
-
-
?
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
-
-
-
additional information
?
-
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
-
additional information
?
-
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC2
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
-
additional information
?
-
Sphingomonas sanxanigenens NX02
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
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
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
M1T754
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
F4NCC2
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Trypanosoma brucei 427
F4NCC2
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Sphingomonas sanxanigenens NX02
M1T754
-
-
-
?
alpha-D-mannose 1-phosphate
D-mannose 6-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
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 6-phosphate
alpha-D-mannose 1-phosphate
show the reaction diagram
Q980S1
it is unclear whether either glucose or mannose phosphate represents the cellular substrate for SsoPHM. The Km values for rSsoPHM toward glucose 6-phosphate and mannose 6-phosphate are in the low millimolar range, significantly higher than that expected for a physiological substrate. Since the protein encoded by sso0207 is the only identifiable phosphohexomutase in the Sulfolbus solfataricus P2 genome, SsoPHM provides the only recognizable avenue for interconverting glucose 6-phosphate and glucose 1-phosphate during glycogen synthesis and breakdown
-
-
r
additional information
?
-
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
additional information
?
-
-
bifunctional enzyme with phosphoglucomutase, EC 5.4.2.2, and phosphomannomutase activities
-
-
-
additional information
?
-
Trypanosoma brucei, Trypanosoma brucei 427
F4NCC2
the enzyme exhibits the function of phosphoglucomutase, EC 5.4.2.2, whose gene is lost in Trypanosoma brucei, together with phosphomannomutase, EC 5.4.2.8, producing D-glucose 1-phosphate from D-glucose 6-phosphate, kinetics, overview
-
-
-
additional information
?
-
Sphingomonas sanxanigenens NX02
M1T754
bifunctional enzyme with phosphoglucomutase and phosphomannomutase, EC 5.4.2.8, activities, the catalytic efficiency is about 15fold higher for glucose 1-phosphate than for mannose 1-phosphate
-
-
-
METALS and IONS
ORGANISM
UNIPROT
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+
Q980S1
divalent metal required, preferentially Mn2+ or Mg2+
Mg2+
-
highest activity in the presence of Mg2+
Mn2+
-
divalent cation required, at 2.0 mM 7% of the activation relative to Mg2+
Mn2+
-
20% relative activity
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+
Q980S1
divalent metal required, preferentially Mn2+ or Mg2+
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
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
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]
SUBSTRATE
ORGANISM
UNIPROT
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
0.327
alpha-D-mannose 1-phosphate
F4NCC2
pH 7.3, 37C
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
0.68
alpha-D-mannose 1-phosphate
M1T754
recombinant His-tagged enzyme, pH 7.6, temperature 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]
SUBSTRATE
ORGANISM
UNIPROT
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
2.28
alpha-D-mannose 1-phosphate
M1T754
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.35
alpha-D-mannose 1-phosphate
M1T754
recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication
638
37
alpha-D-mannose 1-phosphate
F4NCC2
pH 7.3, 37C
638
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0025
Q980S1
pH 6.5, 65C
25
-
using alpha-D-mannose 1-phosphate as substrate, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30C
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 7
Cassia corymbosa
-
-
6.5
Q980S1
assay at
6.5
F4NCC2
-
7
-
10mM Mg2+, 90C
7.1
O80840
95% of maximum activity
7.4
-
-
7.5
Q9KZL6
activity assay
7.5
-
activity assay
7.6
M1T754
assay at
7.8
-
kinetic assay
9
-
around, bicine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
F4NCC2
activity range, inactive above and below
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
ORGANISM
UNIPROT
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
37
F4NCC2
assay at
65
Q980S1
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.12
C0JP35
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
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
additional information
F4NCC2
quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms
Manually annotated by BRENDA team
additional information
Trypanosoma brucei 427
-
quantitative proteomic analysis show that the TbPMM protein is present in both life cycle stages, procyclic and bloodstream forms
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
expression in COS-7 cells
Manually annotated by BRENDA team
F4NCC2
blood stream parasite form
Manually annotated by BRENDA team
Trypanosoma brucei 427
-
blood stream parasite form
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27900
C0JP35
calculated from amino acid sequence
694656
29000
-
immunoprecipitation using 9e10 antibody
3356
38000
-
gel filtration
3353
41000
Cassia corymbosa
-
density gradient ultracentrifugation
3288
50000
-
SDS-PAGE
662065
55000
-
gel filtration
3355
58000
Cassia corymbosa
-
gel filtration
3288
60000
-
gel filtration
3359
62000
-
gel filtration
3350
105400
-
native enzyme, non-denaturing PAGE
692918
210000
-
gel filtration
662018
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
O80840
x * 27700, calculated and MALDI-TOF
?
-
x * 31100, SDS-PAGE
?
Q95ZD7
x * 31100, SDS-PAGE
?
M1T754
x ** 49800, about, sequence calculation
?
Sphingomonas sanxanigenens NX02
-
x ** 49800, about, sequence calculation
-
dimer
-
2 * 30000, SDS-PAGE
dimer
-
2 * 29000
homodimer
-
2 * 51000, SDS-PAGE
tetramer
-
4 * 49850, protein encoded by gene TK1108, calculated
homodimer
Sphingobium chungbukense DJ77
-
2 * 51000, SDS-PAGE
-
additional information
-
structure analysis of the active phosphoenzyme, the inactive dephosphoenzyme, and the phosphoenzyme in complex with the substrate analog xylose 1-phosphate, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
active form of PMM/PGM is phosphorylated at Ser108
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
-
phosphorylation of conserved catalytic active site residue Ser108 has broad effects on residues in multiple domains. Dephosphorylation of the enzyme may play two critical functional roles: a direct role in the chemical step of phosphoryl transfer and secondly through propagation of structural flexibility. Dephosphorylation has minimal effects on crystal structure of the enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
-
purified recombinant detagged enzyme, hanging drop vapor diffusion and microseeding techniques, 1.3 to 1.4 M sodium/potassium tartrate and 100 mM HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 1.8 A resolution, modeling
-
purified recombinant detagged enzyme, hanging drop vapour diffusion, from 2 M (NH4)2SO4, 0.2 M NaCl, 0.1 M sodium cacodylate, pH 6.0, 20C, X-ray diffraction structure determination and analysis at 1.86 A resolution, molecular replacement using a modified form of the Leishmania mexicana enzyme, PDB ID 2i54
F4NCC2
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
maximal stability
3350
TEMPERATURE STABILITY
ORGANISM
UNIPROT
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
3350
50
-
40% loss of activity after 3 min
649781
95
-
longer than 90 min stable
662065
100
-
highly stable, half-life of about 85 min in boiling water in presence of 10mM Mg2+
662018
100
-
50% activity after 5 min
662065
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mg2+ stabilizes
-
higly unstable during storage
-
STORAGE STABILITY
ORGANISM
UNIPROT
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
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 His-tagged enzyme from Escherichia coli strain BL21(DE3), removal of the His-tag, purification by nickel affinity chromatography and dialysis
-
recombinant PGM
-
recombinant PMM/PGM
-
nickel-affinity column chromatography
-
nickel-chelating resin chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
M1T754
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
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration, removal of the His-tag by TEV protease
F4NCC2
ammonium sulfate, Sephadex G-25, KM-cellulose, partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
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
-
expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
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
-
gene pgmG, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), cloning in Escherichia coli strain DH5alpha
M1T754
the vectors pET24ma, pIBR25 and pKC1139 are used
Q9KZL6
overexpression of histidine-tagged fusion protein in Escherichia coli
Q980S1
expression in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
C8CK06, C8CK09, C8CK10
gene PMM, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli
F4NCC2
ENGINEERING
ORGANISM
UNIPROT
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
-
no catalytic activity
R20A
-
12% of wild-type 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
-
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
DELTAmanAB
B6Z254
phosphomannose isomerase, phosphomannosemutase double mutant
additional information
F4NCC2
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
additional information
Trypanosoma brucei 427
-
RNAi knockdown of gene TbPMM, construction of a cell line expressing tetracycline inducible double-stranded RNA targeting TbPMM, induction of dsRNA targeting TbPMM results in a 68% knockdown of TbPMM mRNA after 48 h and a reduction of growth rate that leads to cell death after 72 h, phenotypes, overview
-
APPLICATION
ORGANISM
UNIPROT
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
-
analysis of clinically important mutations involved in congential disorder of glycosylation type 1a
food industry
M1T754
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
food industry
Sphingomonas sanxanigenens NX02
-
the enzyme is involved in production of sphingans, extracellular polysaccharides used as thickeners, emulsifiers and gelling agents, its overexpression increases the sphingan production of the transformed cell
-
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