BRENDA - Enzyme Database show
show all sequences of 5.3.2.5

MtnBD is a multifunctional fusion enzyme in the methionine salvage pathway of Tetrahymena thermophila

Nakano, T.; Ohki, I.; Yokota, A.; Ashida, H.; PLoS ONE 8, e67385 (2013)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-(methylthio)-2,3-dioxopentyl phosphate
Tetrahymena thermophila
-
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Tetrahymena thermophila
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-(methylthio)-2,3-dioxopentyl phosphate
-
728615
Tetrahymena thermophila
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
-
-
?
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-(methylthio)-2,3-dioxopentyl phosphate
Tetrahymena thermophila
-
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-(methylthio)-2,3-dioxopentyl phosphate
-
728615
Tetrahymena thermophila
2-hydroxy-5-(methylthio)-3-oxopent-1-enyl phosphate
-
-
-
?
Other publictions for EC 5.3.2.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
728615
Nakano
MtnBD is a multifunctional fus ...
Tetrahymena thermophila
PLoS ONE
8
e67385
2013
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727007
Warlick
Mechanistic diversity in the R ...
Geobacillus kaustophilus, no activity in Rhodospirillum rubrum
Biochemistry
51
9470-9479
2012
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714022
Nakano
An evolutionally conserved Lys ...
Bacillus subtilis
Biochem. Biophys. Res. Commun.
392
212-216
2010
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1
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3
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2
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1
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2
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2
2
715360
Singh
Roles of RubisCO and the Rubis ...
Rhodospirillum rubrum, Rhodospirillum rubrum Str-2
J. Bacteriol.
192
1324-1331
2010
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1
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1
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2
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6
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3
3
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701475
Tamura
Structure of the apo decarbamy ...
Bacillus subtilis
Acta Crystallogr. Sect. D
65
942-951
2009
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1
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2
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1
1
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693411
Ashida
RuBisCO-like proteins as the e ...
Bacillus subtilis, Geobacillus kaustophilus, Microcystis aeruginosa, Rhodopseudomonas palustris, Rhodospirillum rubrum
J. Exp. Bot.
59
1543-1554
2008
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5
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5
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5
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5
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16
16
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678268
Imker
Mechanistic diversity in the R ...
Bacillus subtilis 168, Bacillus subtilis, Geobacillus kaustophilus
Biochemistry
46
4077-4089
2007
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2
1
3
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2
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6
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86
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2
2
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2
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2
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6
6
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717772
Carre-Mlouka
A new rubisco-like protein coe ...
Microcystis aeruginosa
J. Biol. Chem.
281
24462-24471
2006
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1
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2
2
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718388
Ashida
Was photosynthetic RuBisCO rec ...
Bacillus subtilis
Res. Microbiol.
156
611-618
2005
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3
3
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706755
Ashida
A functional link between RuBi ...
Bacillus subtilis
Science
302
286-290
2003
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3
3
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669181
Myers
Purification and characterizat ...
Klebsiella pneumoniae, Klebsiella pneumoniae CG253
J. Biol. Chem.
268
24785-24791
1993
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