BRENDA - Enzyme Database
show all sequences of 2.7.1.175

Synthesis of alpha-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and maltokinase Pep2

Roy, R.; Usha, V.; Kermani, A.; Scott, D.J.; Hyde, E.I.; Besra, G.S.; Alderwick, L.J.; Fuetterer, K.; ACS Chem. Biol. 8, 2245-2255 (2013)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2, overview
Mycobacterium tuberculosis
Cloned(Commentary)
Cloned (Commentary)
Organism
gene Rv0127 or pep2, recombinant overexpression of His-tagged enzyme in Mycobacterium smegmatis
Mycobacterium tuberculosis
Engineering
Protein Variants
Commentary
Organism
D321A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
K145A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
Q309A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten type kinetics
Mycobacterium tuberculosis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required, residues K145, Q309, and D321 are involved in Mg2+ binding
Mycobacterium tuberculosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
-
Mycobacterium tuberculosis
452900
-
TreS-Pep2 complex, sequence calculation
Mycobacterium tuberculosis
470000
-
TreS-Pep2 complex, ultracentrifugation, Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + maltose
Mycobacterium tuberculosis
-
ADP + alpha-maltose-1-phosphate
-
-
?
ATP + maltose
Mycobacterium tuberculosis ATCC 25618
-
ADP + alpha-maltose-1-phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Mycobacterium tuberculosis
O07177
gene Rv0127
-
Mycobacterium tuberculosis ATCC 25618
O07177
gene Rv0127
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant His-tagged enzyme from Mycobacterium smegmatis by nickel affinity chromatography
Mycobacterium tuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + maltose
-
737320
Mycobacterium tuberculosis
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
-
737320
Mycobacterium tuberculosis ATCC 25618
ADP + alpha-maltose-1-phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
Mycobacterium tuberculosis
trimer or tetramer
x * 52000, ultracentrifugation
Mycobacterium tuberculosis
Synonyms
Synonyms
Commentary
Organism
Pep2
-
Mycobacterium tuberculosis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Mycobacterium tuberculosis
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Mycobacterium tuberculosis
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2, overview
Mycobacterium tuberculosis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Rv0127 or pep2, recombinant overexpression of His-tagged enzyme in Mycobacterium smegmatis
Mycobacterium tuberculosis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Mycobacterium tuberculosis
Engineering (protein specific)
Protein Variants
Commentary
Organism
D321A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
K145A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
Q309A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
Mycobacterium tuberculosis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten type kinetics
Mycobacterium tuberculosis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required, residues K145, Q309, and D321 are involved in Mg2+ binding
Mycobacterium tuberculosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
52000
-
-
Mycobacterium tuberculosis
452900
-
TreS-Pep2 complex, sequence calculation
Mycobacterium tuberculosis
470000
-
TreS-Pep2 complex, ultracentrifugation, Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + maltose
Mycobacterium tuberculosis
-
ADP + alpha-maltose-1-phosphate
-
-
?
ATP + maltose
Mycobacterium tuberculosis ATCC 25618
-
ADP + alpha-maltose-1-phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Mycobacterium smegmatis by nickel affinity chromatography
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + maltose
-
737320
Mycobacterium tuberculosis
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
-
737320
Mycobacterium tuberculosis ATCC 25618
ADP + alpha-maltose-1-phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
Mycobacterium tuberculosis
trimer or tetramer
x * 52000, ultracentrifugation
Mycobacterium tuberculosis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Mycobacterium tuberculosis
General Information
General Information
Commentary
Organism
metabolism
the enzyme PepS is involved in the cytoplasmic GlgE-pathway that converts trehalose to alpha(1->4),alpha(1->6)-linked glucan in 4 steps
Mycobacterium tuberculosis
additional information
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
Mycobacterium tuberculosis
physiological function
the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis, is coated by an alpha-glucan-containing capsule that has been implicated in persistence. Maltokinase Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2. Synthesis of alpha-glucan in mycobacteria involves the heterooctameric complex in the GlgE pathway. The complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients
Mycobacterium tuberculosis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme PepS is involved in the cytoplasmic GlgE-pathway that converts trehalose to alpha(1->4),alpha(1->6)-linked glucan in 4 steps
Mycobacterium tuberculosis
additional information
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
Mycobacterium tuberculosis
physiological function
the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis, is coated by an alpha-glucan-containing capsule that has been implicated in persistence. Maltokinase Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2. Synthesis of alpha-glucan in mycobacteria involves the heterooctameric complex in the GlgE pathway. The complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients
Mycobacterium tuberculosis
Other publictions for EC 2.7.1.175
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
Synonyms
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)
739666
Fraga
Structure of mycobacterial mal ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618, Mycolicibacterium vanbaalenii, Mycolicibacterium vanbaalenii DSM 7251
Sci. Rep.
5
8026
2015
-
-
2
1
15
-
-
-
-
2
-
4
-
6
-
-
2
1
-
-
-
-
4
1
2
3
-
-
-
2
-
-
2
-
-
-
-
-
2
2
1
15
-
-
-
-
-
-
2
-
4
-
-
-
2
-
-
-
-
4
1
3
-
-
-
2
-
-
-
-
5
5
-
-
-
737320
Roy
Synthesis of alpha-glucan in m ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
ACS Chem. Biol.
8
2245-2255
2013
1
-
1
-
3
-
-
1
-
1
3
2
-
7
-
-
1
-
-
-
-
-
2
2
1
-
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
3
-
-
-
-
1
-
1
3
2
-
-
-
1
-
-
-
-
2
2
-
-
-
-
1
-
-
-
-
3
3
-
-
-
717432
Mendes
Biochemical characterization o ...
Mycobacterium tuberculosis variant bovis
BMC Biochem.
11
21
2010
-
1
1
-
-
1
1
3
-
5
1
1
-
5
-
-
1
-
-
-
-
1
4
1
2
1
1
-
-
1
1
-
3
-
-
-
-
1
1
3
-
-
1
-
1
-
3
-
5
1
1
-
-
-
1
-
-
-
1
4
1
1
1
-
-
1
1
-
-
-
2
2
-
-
-
717816
Elbein
Last step in the conversion of ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 14468
J. Biol. Chem.
285
9803-9812
2010
-
1
-
-
-
-
-
-
-
1
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
1
-
-
1
-
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1
-
1
-
-
-
-
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-
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1
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
717739
Jarling
Isolation of mak1 from Actinop ...
Actinoplanes missouriensis, Streptomyces coelicolor, Streptomyces coelicolor A3(2)
J. Basic Microbiol.
44
360-373
2004
-
-
2
-
-
-
-
-
-
1
4
-
-
9
-
-
2
-
-
-
1
-
3
2
2
1
-
-
-
1
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
1
4
-
-
-
-
2
-
-
1
-
3
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
717163
Niehues
Isolation and characterization ...
Actinoplanes missouriensis
Arch. Microbiol.
180
233-239
2003
-
-
-
-
-
-
-
3
-
1
1
-
-
2
-
-
1
-
-
-
-
-
1
1
-
1
1
-
-
2
-
-
2
-
1
-
-
-
-
2
-
-
-
-
-
-
3
-
1
1
-
-
-
-
1
-
-
-
-
1
1
1
1
-
-
2
-
-
1
-
-
-
-
-
-
717600
Drepper
Maltokinase (ATP:maltose 1-pho ...
Actinoplanes sp.
FEBS Lett.
388
177-179
1996
-
-
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-