Information on EC 4.2.3.153 - (5-formylfuran-3-yl)methyl phosphate synthase

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 expected taxonomic range for this enzyme is: Methanocaldococcus jannaschii

EC NUMBER
COMMENTARY hide
4.2.3.153
-
RECOMMENDED NAME
GeneOntology No.
(5-formylfuran-3-yl)methyl phosphate synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 D-glyceraldehyde 3-phosphate = (5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Methane metabolism
-
-
methanofuran biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glyceraldehyde-3-phosphate phosphate-lyase [D-glyceraldehyde-3-phosphate-adding; (5-formylfuran-3-yl)methyl-phosphate-forming]
The enzyme catalyses the reaction in the direction of producing (5-formylfuran-3-yl)methyl phosphate, an intermediate in the biosynthesis of methanofuran. The sequence of events starts with the removal of a phosphate group, followed by aldol condensation and cyclization. Methanofuran is a carbon-carrier cofactor involved in the first step of the methanogenic reduction of carbon dioxide by methanogenic archaea.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 D-glyceraldehyde
3-phosphate(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
show the reaction diagram
2 D-glyceraldehyde 3-phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
show the reaction diagram
D-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
show the reaction diagram
additional information
?
-
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-glyceraldehyde 3-phosphate + glycerone phosphate
(5-formylfuran-3-yl)methyl phosphate + phosphate + 2 H2O
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035 - 0.048
D-glyceraldehyde
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022 - 0.026
D-glyceraldehyde
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46 - 0.74
D-glyceraldehyde
639
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
x * 25000, SDS-PAGE
26053
-
6 * 26053, calculated and crystallization data
171000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular docking of glycerinaldehyde 3-phosphate into the active site
-
to 1.7 A resolution. Enzyme is a member of the TIM-barrel superfamily and the biological unit is a homohexamer
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D151N
-
mutation of strictly conserved residue around the active site, complete inactivation
D25N
-
mutation of strictly conserved residue around the active site, complete inactivation
K155R
-
kcat/KM value comparable to the wild-type
K27R
-
mutation of strictly conserved residue around the active site, complete inactivation
K85R
-
mutation of strictly conserved residue around the active site, complete inactivation
D151N
-
mutation of strictly conserved residue around the active site, complete inactivation
-
D25N
-
mutation of strictly conserved residue around the active site, complete inactivation
-
K155R
-
kcat/KM value comparable to the wild-type
-
K27R
-
mutation of strictly conserved residue around the active site, complete inactivation
-
K85R
-
mutation of strictly conserved residue around the active site, complete inactivation
-
Show AA Sequence (151 entries)
Please use the Sequence Search for a specific query.