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Information on EC 5.3.1.23 - S-methyl-5-thioribose-1-phosphate isomerase
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5.3.1.23 S-methyl-5-thioribose-1-phosphate isomeraseSpecify your search results
Word Map
- 5.3.1.23
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salvage
- phosphorylase
- mta
- dehydratase
- s-adenosylmethionine
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ribose-1,5-bisphosphate
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mill
- 5'-deoxy-5'-methylthioadenosine
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aci-reductone
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universally
- avocado
- persea
- nucleosidase
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auxotrophic
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klebsiella
- transaminase
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pyrococcus
- horikoshii
- americana
- polyamine
- brewing
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
mtr-1-p, ph0702, ypr118w, methylthioribose-1-phosphate isomerase, 5'-methylthioribose-1-phosphate isomerase, 5-methylthioribose-1-phosphate isomerase, 5-methylthioribose 1-phosphate isomerase, meu1p, bs-m1pi, 1-pmtr isomerase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-PMTR isomerase
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5'-methylthioribose-1-phosphate isomerase
5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase
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5-methylthioribose 1-phosphate isomerase
5-methylthioribose-1-phosphate isomerase
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Bs-M1Pi
Isomerase, methylthioribose 1-phosphate
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M1Pi
methylthioribose-1-phosphate isomerase
MRDI
MRI1
mtnA
MTR-1-P
MTR-1-P isomerase
PH0702
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
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S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
catalytic reaction mechanism, structure-function relationship, overview. Proposed reaction mechanism of M1Pi proceeds via a cis-phosphoenolate intermediate and through the following steps: (1) transfer of proton from Asp247 to the O4 atom of MTR-1-P, (2) proton abstraction from C2 atom of the substrate by the thiolate anion of Cys167 as well as cleavage of the C1-O4 bond, (3) simultaneous proton abstraction from O2 atom by the deprotonated Asp247 and transfer of proton from the thiol group of Cys167 to C1 atom, and (4) generation of the product, MTRu-1-P
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
proposed reaction mechanism probably including residue Asp240, overview
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism, overview
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
proposed reaction mechanism probably including residue Asp240, overview
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S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
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isomerization
isomerization
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase
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CAS REGISTRY NUMBER
COMMENTARY
91608-95-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
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r
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
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-
-
?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
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-
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme of the pathway of the conversion of methylthioribose-1-phosphate to methionine
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme in synthesis of methionine from 5'-S-methylthioadenosine
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme in synthesis of methionine from 5'-S-methylthioadenosine
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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-
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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-
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
additional information
?
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substrate MTR-1-P is synthesized from S-adenosyl-L-methionine through hydrolysis of the adenine base by HCl, and C1 of the ribose moiety is phosphorylated by ATP via MtnK, an MTR kinase. MTR-1-P isomerase is assayed in a coupling reaction with MtnB and MtnW, previously identified as MTRu-1-P dehydratase and 2,3-diketo-5-methylthiopentyl-1-phosphate enolase respectively. In this assay, the reaction product MTRu-1-P is converted to 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) by sequential reactions of MtnB and MtnW. NMR analysis of the MtnA reaction product, overview
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additional information
?
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substrate MTR-1-P is synthesized from S-adenosyl-L-methionine through hydrolysis of the adenine base by HCl, and C1 of the ribose moiety is phosphorylated by ATP via MtnK, an MTR kinase. MTR-1-P isomerase is assayed in a coupling reaction with MtnB and MtnW, previously identified as MTRu-1-P dehydratase and 2,3-diketo-5-methylthiopentyl-1-phosphate enolase respectively. In this assay, the reaction product MTRu-1-P is converted to 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) by sequential reactions of MtnB and MtnW. NMR analysis of the MtnA reaction product, overview
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additional information
?
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substrate MTR-1-P is synthesized from S-adenosyl-L-methionine through hydrolysis of the adenine base by HCl, and C1 of the ribose moiety is phosphorylated by ATP via MtnK, an MTR kinase. MTR-1-P isomerase is assayed in a coupling reaction with MtnB and MtnW, previously identified as MTRu-1-P dehydratase and 2,3-diketo-5-methylthiopentyl-1-phosphate enolase respectively. In this assay, the reaction product MTRu-1-P is converted to 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) by sequential reactions of MtnB and MtnW. NMR analysis of the MtnA reaction product, overview
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme of the pathway of the conversion of methylthioribose-1-phosphate to methionine
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme in synthesis of methionine from 5'-S-methylthioadenosine
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?
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
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enzyme in synthesis of methionine from 5'-S-methylthioadenosine
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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?
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
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r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
M1Pi does not require any metals to exhibit catalytic activity
additional information
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M1Pi does not require any metals to exhibit catalytic activity
additional information
enzyme M1Pi does not require any metals to exhibit its catalytic activity
additional information
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enzyme M1Pi does not require any metals to exhibit its catalytic activity
additional information
the activity is not at all influenced by EDTA treatment, indicating that the Bacillus subtilis MTR-1-P isomerase does not require a metal ion for its catalysis
additional information
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the activity is not at all influenced by EDTA treatment, indicating that the Bacillus subtilis MTR-1-P isomerase does not require a metal ion for its catalysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Proteomic analysis of infiltrating ductal carcinoma tissues by coupled 2-D DIGE/MS/MS analysis.
Neoplasms
Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits.
Neoplasms
Proteomic analysis of infiltrating ductal carcinoma tissues by coupled 2-D DIGE/MS/MS analysis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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clone A has 5-methylthioribose-1-phosphate isomerase activity, clone D lacks this enzyme
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the family PF01008. The open and closed states of the proteins belonging to the family PF01008 are usually demarcated by the degree of angle formed owing to the bend in the longest helix alpha5
metabolism
physiological function
additional information
metabolism
the enzyme is part of the methionine salvage pathway (MSP) is a metabolic pathway for recovery of the reduced sulfur in 5-methylthioribose (MTR), which is formed in the synthesis of polyamines, as methionine
metabolism
the methionine salvage pathway (MSP) plays a crucial role in recycling a sulfhydryl derivative of the nucleoside. In MSP of Bacillus subtilis, the 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P)
metabolism
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the enzyme is part of the methionine salvage pathway (MSP) is a metabolic pathway for recovery of the reduced sulfur in 5-methylthioribose (MTR), which is formed in the synthesis of polyamines, as methionine
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metabolism
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the methionine salvage pathway (MSP) plays a crucial role in recycling a sulfhydryl derivative of the nucleoside. In MSP of Bacillus subtilis, the 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P)
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physiological function
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MRDI is induced in metastatic cells by constitutive RhoA activation and promotes cell invasion
physiological function
enzyme MtnA of Bacillus subtilis catalyzes the isomerization of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). The reaction is an isomerization of an aldose phosphate harboring a phosphate group on the hemiacetal group
physiological function
in the methionine salvage pathway (MSP) of Bacillus subtilis, 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes an interconversion of 5-methylthioribose 1-phosphate (MTR-1-P) and 5-methylthioribulose 1-phosphate (MTRu-1-P), classified as an aldose-ketose isomerase reaction
physiological function
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enzyme MtnA of Bacillus subtilis catalyzes the isomerization of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). The reaction is an isomerization of an aldose phosphate harboring a phosphate group on the hemiacetal group
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physiological function
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in the methionine salvage pathway (MSP) of Bacillus subtilis, 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes an interconversion of 5-methylthioribose 1-phosphate (MTR-1-P) and 5-methylthioribulose 1-phosphate (MTRu-1-P), classified as an aldose-ketose isomerase reaction
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additional information
enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor
additional information
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enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor
additional information
transition from an open to closed state creates a hydrophobic active site environment. The active-site pocket of M1Pi is optimized to follow a reaction mechanism via the formation of a cis-phosphoenolate intermediate, structural transition, overview
additional information
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enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
additional information
enzyme structure and active site structure comparisons, open/closed conformational transition of enzyme M1Pi. The structure of Bs-M1Pi shows that the active site is completely shielded from the solvent region. The substrate binding is likely to induce the large conformational changes of N- and C-terminal domains as well as the rearrangement of the hydrogen-bond network around the loops 93-98 and 290-294 to stabilize the closed state of the enzyme
additional information
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enzyme structure and active site structure comparisons, open/closed conformational transition of enzyme M1Pi. The structure of Bs-M1Pi shows that the active site is completely shielded from the solvent region. The substrate binding is likely to induce the large conformational changes of N- and C-terminal domains as well as the rearrangement of the hydrogen-bond network around the loops 93-98 and 290-294 to stabilize the closed state of the enzyme
additional information
-
enzyme structure and active site structure comparisons, open/closed conformational transition of enzyme M1Pi. The structure of Bs-M1Pi shows that the active site is completely shielded from the solvent region. The substrate binding is likely to induce the large conformational changes of N- and C-terminal domains as well as the rearrangement of the hydrogen-bond network around the loops 93-98 and 290-294 to stabilize the closed state of the enzyme
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additional information
enzyme three-dimensional structure analysis and structure comparisons. The most visible difference between the open and closed conformation can be perceived in the position of the loop connecting the helices alpha3 and alpha4 of the NTD. In the open state, the loop is away from the active-site pocket, whereas in the closed state the loop moves toward the active-site pocket with a forward shift of about 24 A
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cocrystallized with the substrate 5-methylthio-5-deoxy-D-ribose 1-phosphate, sitting drop vapour diffusion method, using 0.2 M K formate and 15% (w/v) polyethylene glycol 3350, at 20°C
purified enzyme in complex with product S-methyl-1-thio-D-ribulose 1-phosphate or a sulfate ion, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM Na HEPES, pH 7.4, and 1 mM EDTA, with or without 33 mM MTR-1-P, with 0.004-0.006 ml of reservoir solution containing 0.2 M K formate and 15% w/v PEG 3350, 20°C, X-ray diffraction structure determination and analysis at 2.4 A and 2.7 A resolution, respectively. The asymmetric unit contains two dimers for the MTRu-1-P-bound form, while one dimer is found in the asymmetric unit for the sulfate-bound form. Molecular replacement method using the crystal structure of Ypr118w (RCSB, PDB ID 1W2W) as a search model, and modeling
sitting-drop vapour-diffusion method. Crystals diffract to 2.5 A at 100 K using synchrotron radiation and belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2 A, c = 154.7 A
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hanging drop vapor diffusion method, using 0.7 M sodium citrate and 100 mM imidazole, pH 8.0
in silico analysis of conserved residues and molecular modeling of structure. Residues of the enzymic activity of methylthioribose-1-phosphate isomerase that interact with the substrate are absolutely conserved. Residues essential for the hydrophobic stabilization of the substrate/product in the active site are conserved as well
purified recombinant enzyme in two different forms of crystals belonging to space groups P3221 and P1, that are obtained at 4°C and 20°C, respectively. The crystal belonging to space group P3221 grows in a microbatch-under-oil set up by mixing 0.002 ml of protein solution and 0.002 ml of 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 2.5 M 1,6-hexanediol. Initial crystals belonging to space group P1 are obtained by hanging-drop vapor-diffusion method, mixing of 0.003 ml of protein solution with 0.001 ml of resevoir solution containing 0.05 M ammonium acetate, 0.1 M Tris, pH 8.0, 16% PEG 10000 and 0.05 M sodium acetate, method optimization, X-ray diffraction structure determination analysis at 2.30-2.65 A resolution, molecular replacement method using the three-dimensional atomic coordinates of M1Pi from Archaeoglobus fulgidus (PDB ID 1T5O) as the search model, modeling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by nickel-nitrilotriacetic acid affinity chromatography, the His-tag is removed by treatment with tobacco etch virus protease
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recombinant His-tagged enzyme from Escherichia coli strain Rosetta(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off by thrombin, followed by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mtnA, sequence comparisons and phylogenetic tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
into pCMV plasmid for expression in mammalian cells and into pMS356 plasmid for esxpression in Escherichia coli
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Orf PH0702, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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