Information on EC 5.3.1.28 - D-sedoheptulose 7-phosphate isomerase

Word Map on EC 5.3.1.28
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.28
-
RECOMMENDED NAME
GeneOntology No.
D-sedoheptulose 7-phosphate isomerase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ADP-L-glycero-beta-D-manno-heptose biosynthesis
-
-
GDP-D-glycero-alpha-D-manno-heptose biosynthesis
-
-
Lipopolysaccharide biosynthesis
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glycero-D-manno-heptose 7-phosphate aldose-ketose-isomerase
In Gram-negative bacteria the enzyme is involved in biosynthesis of ADP-L-glycero-beta-D-manno-heptose, which is utilized for assembly of the lipopolysaccharide inner core. In Gram-positive bacteria the enzyme is involved in biosynthesis of GDP-D-glycero-alpha-D-manno-heptose, which is required for assembly of S-layer glycoprotein.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
K12
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
serovars Lai and Copenhageni
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
phosphoheptose isomerase of Leptospira is vital for lipopolysaccharide biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
additional information
?
-
the gmhA gene product is essential for the expression of wild-type lipooligosaccharide by this pathogen
-
-
-
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-sedoheptulose 7-phosphate
D-glycero-alpha,beta-D-manno-heptose 7-phosphate
show the reaction diagram
D-sedoheptulose 7-phosphate
D-glycero-D-manno-heptose 7-phosphate
show the reaction diagram
additional information
?
-
O87340
the gmhA gene product is essential for the expression of wild-type lipooligosaccharide by this pathogen
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
the enzyme contains a zinc ion at the heart of its active site, this ion stabilizes the active, closed form of the enzyme and presents coordinating side chains as a potential acid and base to drive catalysis
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-[(1R)-1-hydroxy-2-(phosphonoamino)ethyl]-D-lyxopyranose
-
-
5-[(1R)-2-[4,5-bis(hydroxymethyl)-1H-1,2,3-triazol-1-yl]-1-hydroxyethyl]-D-lyxopyranose
-
poor inhibitor
5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-D-lyxopyranose
-
-
5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-D-lyxopyranose
-
-
5-{(1R)-1-hydroxy-2-[(methylsulfonyl)amino]ethyl}-D-lyxopyranose
-
poor inhibitor
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
-
methyl 5-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-xylopyranoside
-
-
methyl 5-[(1R,2R)-2-carboxy-1,2-dihydroxyethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-alpha-D-lyxopyranoside
-
poor inhibitor
methyl 5-[(1S,2S)-1,2-dihydroxy-2-phosphonoethyl]-alpha-D-lyxopyranoside
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 1.2
D-sedoheptulose 7-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 0.5
D-sedoheptulose 7-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07 - 1.2
D-sedoheptulose 7-phosphate
3626
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia pseudomallei (strain K96243)
Burkholderia pseudomallei (strain K96243)
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20600
x * 20600, calculated from sequence
21495
x * 21495, calculated from sequence
22000
-
x * 22000, SDS-PAGE
25000
x * 25000, SDS-PAGE
29000
-
2 * 29000, SDS-PAGE
60000 - 80000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 29000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method at room temperature, the crystal belong to the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 61.3, b = 84.2, c = 142.3 A
-
untagged enzyme, hanging drop vapor diffusion method, using 0.1 M Na-acetate, pH 4.6, 8% (w/v) PEG 4000
-
hanging drop vapor diffusion method, crystal structures of GmhA in apo, substrate, and product-bound forms
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-agarose column chromatography and Superdex 200 gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pLS88 vector
expressed in Escherichia coli Rosetta (DE3) cells
-
expression in Escherichia coli
overexpressed in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D61A
-
the mutant exhibits about 17fold reduced catalytic efficiency compared to the wild type enzyme
H64Q
-
the mutant exhibits 12fold reduced catalytic efficiency compared to the wild type enzyme
D61A
-
the mutant exhibits about 17fold reduced catalytic efficiency compared to the wild type enzyme
-
D169N
-
inactive
D94N
-
kcat/Km for D-sedoheptulose 7-phosphate is 1.8fold higher than wild-type value
E65N
-
inactive
H180Q
-
inactive
H61Q
-
kcat/Km for D-sedoheptulose 7-phosphate is 2.5fold lower than wild-type value
Q172E
-
inactive
R69Q
-
inactive
T120A
-
inactive
additional information
Glu64, His181, Thr169, Thr122 and His60 are critical for enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
determination of the three-dimensional structure of GmhA from Burkholderia pseudomallei to provide a structural template for the development of antibiotic adjuvants as antimelioidosis agents
Show AA Sequence (4839 entries)
Please use the Sequence Search for a specific query.