Information on EC 5.3.1.8 - mannose-6-phosphate isomerase and Organism(s) Homo sapiens

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Homo sapiens


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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
5.3.1.8
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RECOMMENDED NAME
GeneOntology No.
mannose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Mannose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
hydride transfer mechanism of a alpha-hydrogen bond between the C1 and C2 positions of substrate. Mechanism involves Zn2+ mediating the movement of a proton between O1 and O2, and the hydrophobic environment formed in part by T278 promoting transfer of a hydride ion
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,5-anhydrofructose degradation
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beta-(1,4)-mannan degradation
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beta-1,4-D-mannosyl-N-acetyl-D-glucosamine degradation
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D-mannose degradation
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GDP-mannose biosynthesis
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L-ascorbate biosynthesis I (L-galactose pathway)
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mannitol biosynthesis
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mannitol degradation II
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d-mannose degradation
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Fructose and mannose metabolism
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Amino sugar and nucleotide sugar metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
D-mannose-6-phosphate aldose-ketose-isomerase
A zinc protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-88-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-mannose 6-phosphate
beta-D-fructose 6-phosphate
show the reaction diagram
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r
D-Fructose 6-phosphate
?
show the reaction diagram
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Fructose 6-phosphate
?
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
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recombinant enzyme expressed in E. coli contains slightly less than 1 mol of zinc per mol of proteins
Zn2+
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zinc-dependent metalloenzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5-phospho-D-arabinonhydrazide
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; in 50 mM HEPES buffer, pH 7.1, at 25C
5-phospho-D-arabinonohydroxamic acid
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in 50 mM HEPES buffer, pH 7.1, at 25C; nanomolar inhibitor
arabinose 5-phosphate
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dithiothreitol
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EDTA
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erythrose 4-phosphate
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fructose 1-phosphate
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competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00043
beta-D-mannose 6-phosphate
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in 50 mM HEPES buffer, pH 7.1, at 25C
0.23 - 0.25
mannose 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 6
beta-D-mannose 6-phosphate
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in 50 mM HEPES buffer, pH 7.1, at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
840
beta-D-mannose 6-phosphate
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in 50 mM HEPES buffer, pH 7.1, at 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006
5-phospho-D-arabinonhydrazide
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in 50 mM HEPES buffer, pH 7.1, at 25C
0.000041
5-phospho-D-arabinonohydroxamic acid
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in 50 mM HEPES buffer, pH 7.1, at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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skeletal
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46520
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calculation from nucleotide sequence encoded by cDNA
46530
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recombinant enzyme, electrospray mass spectroscopy
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and refinement by energy minimization and molecular dynamics
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli
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expressed in Escherichia coli GI724 cells
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