Information on EC 4.2.1.109 - methylthioribulose 1-phosphate dehydratase

New: Word Map on EC 4.2.1.109
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
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: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.2.1.109
-
RECOMMENDED NAME
GeneOntology No.
methylthioribulose 1-phosphate dehydratase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-5-thio-D-ribulose 1-phosphate = 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydration
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
methionine metabolism
-
-
S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
S-methyl-5-thio-D-ribulose-1-phosphate 4-hydro-lyase [5-(methylthio)-2,3-dioxopentyl-phosphate-forming]
This enzyme forms part of the methionine-salvage pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 168 (trp C2)
TrEMBL
Manually annotated by BRENDA team
Bacillus subtilis 168 (trp C2)
strain 168 (trp C2)
TrEMBL
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene Yjr024cp by homology comparison
SwissProt
Manually annotated by BRENDA team
gene mtnBD
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the MtnB domain of Tetrahymena thermophila MtnBD acquired the new function to catalyze both the dehydratase and enolase reactions through evolutionary gene mutations, rather than fusion of MSP genes
malfunction
the enzyme depletion specifically impairs the capacity of cells to grow in media where methionine is replaced by 5-methylthioadenosine. Knockdown of the enzyme specifically affects the recycling of methionine, and mutation of three potential phosphorylation sites does not affect the enzyme activity whereas mutation of the potential zinc binding site completely abrogates it
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-methyl-5-thio-D-ribulose 1-phosphate
5-(methylthio)-2,3-dioxopentyl phosphate + H2O
show the reaction diagram
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
S-methyl-5-thio-D-ribulose 1-phosphate
5-(methylthio)-2,3-dioxopentyl phosphate + H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0089
S-methyl-5-thio-D-ribulose 1-phosphate
25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16.5
S-methyl-5-thio-D-ribulose 1-phosphate
Bacillus subtilis
O31668
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
at 55C the enzyme loses most of its activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 55
at 55C the enzyme loses most of its activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
without His-tag, 4 * 23800, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme fragment of residues 20-242, hanging drop vapour diffusion method, 0.001 ml of protein solution, containing 20 mM Tris-HCl, 5% v/v glycerol, 0.1 mM TCEP, 100 mM sodium chloride, pH 8.0, is mixed with 0.001 ml of reservoir solution, containing 0.04 M citric acid, 0.06 M Bis-Tris propane, 5% v/v glycerol, 18-21% w/v PEG 3350, and equilibrated against 0.2 ml of reservoir solution, 22C, 5 days to 2 weeks, X-ray diffraction structure determination and analysis at 2.40 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homogeneity, using the His-tag, the His-tag is cleaved with thrombin
recombinant His-tagged enzyme residues 20-242 from Escherichia coli strain Rosetta 2(DE3) by metal affinity chhromatography, anion exchange chromatography, gel filtration, and ultrafiltration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as (His)6-tagged soluble protein in Escherichia BL21 (DE3), vector pET15b
gene mtnBD, identification of the domains responsible for catalyzing the four reactions from the enzyme, overview. Recombinant expression of His-tagged proteins of full-length enzyme and the MtnB domain in Escherichia coli BL21(DE3)
recombinant overexpression of an His-tagged enzyme fragment comprising the residues 20-242 in Escherichia coli strain Rosetta 2(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D72A
-
site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme
D72A/K90A
-
site-directed mutagenesis, the mutant shows a similar level of pyroptosis inhibition as the wild-type enzyme, but a significant loss of apoptosis inhibition activity
K90A
-
site-directed mutagenesis, the mutant shows a similar level of pyroptosis inhibition as the wild-type enzyme, but a significant loss of apoptosis inhibition activity
P185A
-
site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme
Y184A
-
site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme
Y184A/P185A
-
site-directed mutagenesis, the mutant shows similar levels of pyroptosis inhibition and apoptosis inhibition as the wild-type enzyme
additional information
Show AA Sequence (2587 entries)
Please use the Sequence Search for a certain query.