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ATP + maltose
ADP + alpha-maltose 1-phosphate
-
-
product analysis and determination by chemical analysis and NMR spectroscopy
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
ATP + maltose
ADP + maltose 1-phosphate
GTP + maltose
GDP + maltose 1-phosphate
-
-
NMR spectroscopical product analysis
-
?
UTP + maltose
UDP + maltose 1-phosphate
-
-
NMR spectroscopical product analysis
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + alpha-maltose-1-phosphate
-
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
-
-
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
maltose cannot be replaced by spectinomycin, streptomycin, kasugamycin, kanamycin, hygromycin, or apramycin as a phosphoryl-group acceptor
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
-
-
NMR spectroscopical product analysis
-
?
ATP + maltose
ADP + maltose 1-phosphate
-
-
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
-
-
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
maltotriose, maltotetraose, L-arabinose, inositol, cellobiose, L-lactose, D-mannose, raffinose, or trehalose cannot replace maltose as a phosphorylgroup acceptor in the reaction catalyzed by Pep2. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor
-
-
?
ATP + maltose
ADP + maltose 1-phosphate
maltotriose, maltotetraose, L-arabinose, inositol, cellobiose, L-lactose, D-mannose, raffinose, or trehalose cannot replace maltose as a phosphorylgroup acceptor in the reaction catalyzed by Pep2. ATP cannot be replaced by other nucleotides as a phosphoryl-group donor
-
-
?
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evolution
-
genetic environment of the mak gene in different organisms. Organization of the region containing the mak gene, overview
evolution
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview
evolution
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview
evolution
-
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview
-
evolution
-
the enzyme belongs to the family of eukaryotic-like kinases (ELKs) with N-terminal domain topologically resembling the cystatin family of protease inhibitors. Phylogenetic analysis, overview
-
metabolism
-
involvement of maltose-1-phosphate in the regulation of sugar metabolism in Escherichia coli
metabolism
-
the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose
metabolism
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan
metabolism
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan
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
metabolism
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
metabolism
-
the enzyme is involved in a pathway of glycogen synthesis using trehalose as the source of glucose
-
metabolism
-
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
-
metabolism
-
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan
-
metabolism
-
the enzyme catalyzes the fourth and last step of the GlcE pathway that channels trehalose to glycogen synthesis and is also likely involved in the biosynthesis of two other crucial polymers: intracellular methylglucose lipopolysaccharides and exposed capsular glucan
-
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
-
metabolism
-
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
-
physiological function
maltokinase is the enzyme responsible for the ATP-dependent formation of maltose 1-phosphate
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
physiological function
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
physiological function
-
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
-
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
-
physiological function
-
the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2
-
additional information
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
additional information
-
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
additional information
the enzyme shows an eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases, a typical eukaryotic protein kinase-like fold. Subtle structural rearrangements occur upon nucleotide binding in the cleft between the N- and the C-terminal lobes. The enzyme has a phosphate-binding region in the N-terminal lobe that is proposed to act as an anchoring point tethering maltokinase and trehalose isomerase activities to the site of glycogen biosynthesis, ensuring correct regulation of Mak activity and possibly preventing excessive accumulation of maltose 1-phosphate. The enzyme's unusual N-terminal domain, with the 146AMLKV150 motif, containing the conserved phosphate-binding lysine residue, might regulate its phosphotransfer activity and represents the most likely anchoring point for TreS, the upstream enzyme in the pathway. Putative catalytic base is residue Asp305
additional information
enzyme complex structure analysis and location of active sites, overview
additional information
-
enzyme complex structure analysis and location of active sites, overview
additional information
-
enzyme complex structure analysis and location of active sites, overview
-
additional information
-
the enzyme shows an eukaryotic-like kinase (ELK) fold, similar to methylthioribose kinases and aminoglycoside phosphotransferases, a typical eukaryotic protein kinase-like fold. Subtle structural rearrangements occur upon nucleotide binding in the cleft between the N- and the C-terminal lobes. The enzyme has a phosphate-binding region in the N-terminal lobe that is proposed to act as an anchoring point tethering maltokinase and trehalose isomerase activities to the site of glycogen biosynthesis, ensuring correct regulation of Mak activity and possibly preventing excessive accumulation of maltose 1-phosphate. The enzyme's unusual N-terminal domain, with the 146AMLKV150 motif, containing the conserved phosphate-binding lysine residue, might regulate its phosphotransfer activity and represents the most likely anchoring point for TreS, the upstream enzyme in the pathway. Putative catalytic base is residue Asp305
-
additional information
-
stoichiometry of the TreS-Pep2 complex, analytical ultracentrifugation, overview
-
additional information
-
enzyme complex structure analysis and location of active sites, overview
-
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452900
TreS-Pep2 complex, sequence calculation
470000
TreS-Pep2 complex, ultracentrifugation, Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
49800
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
50700
-
1 * 50700, recombinant His-tagged Mak, SDS-PAGE
52400
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
53000
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
57000
-
1 * 57000, SDS-PAGE
62000
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
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?
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
-
1 * 57000, SDS-PAGE
monomer
-
1 * 50700, recombinant His-tagged Mak, SDS-PAGE
trimer or tetramer
x * 52000, ultracentrifugation
trimer or tetramer
-
x * 52000, ultracentrifugation
-
additional information
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
additional information
-
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
additional information
-
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
-
additional information
in the TreS:Pep2 complex crystal, diamond-shaped TreS tetramer forms the core of the complex and pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration, but the prevalent stoichiometry in solution is 4 TreS + 2 Pep2 protomers. The behavior in the solution state may be explained by the relatively weak affinity of Pep2 for TreS (Kd 3.5 microM at mildly acidic pH) and crystal packing favoring the 4 + 4 complex. Pep2 forms intimate contacts with the TreS tetramer, revealing a high level of shape complementarity between the binding partners. Structure model, overview. Secondary structure elements contributing to the binding interface are helices alpha5, alpha6, and alpha10 in the C-terminal lobe of Pep2, and contacts made by the N-terminal lobe include residues in helix alpha2, in strand beta8, and in the beta9-beta10 loop. In addition, contacts also involve the beta12-alpha5 loop, which links the N- and C-terminal lobes. The binding interface is dominated by van der Waals and hydrophobic contacts, corresponding to about 70% of surface area buried in the interface per Pep2 monomer
additional information
-
in the TreS:Pep2 complex crystal, diamond-shaped TreS tetramer forms the core of the complex and pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration, but the prevalent stoichiometry in solution is 4 TreS + 2 Pep2 protomers. The behavior in the solution state may be explained by the relatively weak affinity of Pep2 for TreS (Kd 3.5 microM at mildly acidic pH) and crystal packing favoring the 4 + 4 complex. Pep2 forms intimate contacts with the TreS tetramer, revealing a high level of shape complementarity between the binding partners. Structure model, overview. Secondary structure elements contributing to the binding interface are helices alpha5, alpha6, and alpha10 in the C-terminal lobe of Pep2, and contacts made by the N-terminal lobe include residues in helix alpha2, in strand beta8, and in the beta9-beta10 loop. In addition, contacts also involve the beta12-alpha5 loop, which links the N- and C-terminal lobes. The binding interface is dominated by van der Waals and hydrophobic contacts, corresponding to about 70% of surface area buried in the interface per Pep2 monomer
additional information
-
in the TreS:Pep2 complex crystal, diamond-shaped TreS tetramer forms the core of the complex and pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration, but the prevalent stoichiometry in solution is 4 TreS + 2 Pep2 protomers. The behavior in the solution state may be explained by the relatively weak affinity of Pep2 for TreS (Kd 3.5 microM at mildly acidic pH) and crystal packing favoring the 4 + 4 complex. Pep2 forms intimate contacts with the TreS tetramer, revealing a high level of shape complementarity between the binding partners. Structure model, overview. Secondary structure elements contributing to the binding interface are helices alpha5, alpha6, and alpha10 in the C-terminal lobe of Pep2, and contacts made by the N-terminal lobe include residues in helix alpha2, in strand beta8, and in the beta9-beta10 loop. In addition, contacts also involve the beta12-alpha5 loop, which links the N- and C-terminal lobes. The binding interface is dominated by van der Waals and hydrophobic contacts, corresponding to about 70% of surface area buried in the interface per Pep2 monomer
-
additional information
-
in the TreS:Pep2 complex crystal, diamond-shaped TreS tetramer forms the core of the complex and pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration, but the prevalent stoichiometry in solution is 4 TreS + 2 Pep2 protomers. The behavior in the solution state may be explained by the relatively weak affinity of Pep2 for TreS (Kd 3.5 microM at mildly acidic pH) and crystal packing favoring the 4 + 4 complex. Pep2 forms intimate contacts with the TreS tetramer, revealing a high level of shape complementarity between the binding partners. Structure model, overview. Secondary structure elements contributing to the binding interface are helices alpha5, alpha6, and alpha10 in the C-terminal lobe of Pep2, and contacts made by the N-terminal lobe include residues in helix alpha2, in strand beta8, and in the beta9-beta10 loop. In addition, contacts also involve the beta12-alpha5 loop, which links the N- and C-terminal lobes. The binding interface is dominated by van der Waals and hydrophobic contacts, corresponding to about 70% of surface area buried in the interface per Pep2 monomer
-
additional information
the N-terminal lobe can be divided into two subdomains: a cap N-terminal subdomain comprising the first 88 amino acid residues and an intermediate subdomain composed of an anti-parallel beta-sheet flanked by two helices. The C-terminal lobe is mostly alpha-helical. While the N-terminal cap subdomain and the C-terminal lobe are predominantly acidic, the intermediate subdomain is enriched in positively charged residues. The N-terminal cap subdomain is composed of three long antiparallel beta-strands forming a curved beta-sheet that encloses the N-terminal alpha-helix and a short two-stranded beta-sheet running perpendicular to the longest beta-sheet axis, on its concave surface. The intermediate subdomain (residues 89-200) contains a central seven-stranded beta-sheet flanked by two alpha-helical segments. A nine-residue linker (residues 201-209) containing a short beta-strand connects the intermediate subdomain and the C-terminal lobe. This last domain is composed of two central 4-helical bundles, a short beta-hairpin and a small two-stranded beta-sheet
additional information
-
the N-terminal lobe can be divided into two subdomains: a cap N-terminal subdomain comprising the first 88 amino acid residues and an intermediate subdomain composed of an anti-parallel beta-sheet flanked by two helices. The C-terminal lobe is mostly alpha-helical. While the N-terminal cap subdomain and the C-terminal lobe are predominantly acidic, the intermediate subdomain is enriched in positively charged residues. The N-terminal cap subdomain is composed of three long antiparallel beta-strands forming a curved beta-sheet that encloses the N-terminal alpha-helix and a short two-stranded beta-sheet running perpendicular to the longest beta-sheet axis, on its concave surface. The intermediate subdomain (residues 89-200) contains a central seven-stranded beta-sheet flanked by two alpha-helical segments. A nine-residue linker (residues 201-209) containing a short beta-strand connects the intermediate subdomain and the C-terminal lobe. This last domain is composed of two central 4-helical bundles, a short beta-hairpin and a small two-stranded beta-sheet
-
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D321A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
E340R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
K145A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
N145A
site-directed mutagenesis, inactive mutant
Q309A
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
R351A
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
S144A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
D321A
-
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
-
D339N
-
inactive mutant
-
E340R
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
K145A
-
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
-
N145A
-
site-directed mutagenesis, inactive mutant
-
Q309A
-
site-directed mutagenesis, the Mg2+ binding residue mutant is inactive
-
R351A
-
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
-
S144A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
E324R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
K413A
site-directed mutagenesis
N137A
site-directed mutagenesis, inactive mutant
R334R
site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme
S136A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
Y416A
site-directed mutagenesis
Y416F
site-directed mutagenesis
Y420A
site-directed mutagenesis
Y420F
site-directed mutagenesis
N137A
-
site-directed mutagenesis, inactive mutant
-
S136A
-
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
-
Y416A
-
site-directed mutagenesis
-
Y420A
-
site-directed mutagenesis
-
Y420F
-
site-directed mutagenesis
-
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Niehues, B.; Jossek, R.; Kramer, U.; Koch, A.; Jarling, M.; Schroeder, W.; Pape, H.
Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis
Arch. Microbiol.
180
233-239
2003
Actinoplanes missouriensis
brenda
Mendes, V.; Maranha, A.; Lamosa, P.; da Costa, M.S.; Empadinhas, N.
Biochemical characterization of the maltokinase from Mycobacterium bovis BCG
BMC Biochem.
11
21
2010
Mycobacterium tuberculosis variant bovis
brenda
Drepper, A.; Peitzmann, R.; Pape, H.
Maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes sp.: demonstration of enzyme activity and characterization of the reaction product
FEBS Lett.
388
177-179
1996
Actinoplanes sp.
brenda
Jarling, M.; Cauvet, T.; Grundmeier, M.; Kuhnert, K.; Pape, H.
Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase
J. Basic Microbiol.
44
360-373
2004
Streptomyces coelicolor (O54204), Streptomyces coelicolor, Actinoplanes missouriensis (Q7WUM3), Actinoplanes missouriensis, Streptomyces coelicolor A3(2) (O54204)
brenda
Elbein, A.D.; Pastuszak, I.; Tackett, A.J.; Wilson, T.; Pan, Y.T.
Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen
J. Biol. Chem.
285
9803-9812
2010
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 14468
brenda
Roy, R.; Usha, V.; Kermani, A.; Scott, D.J.; Hyde, E.I.; Besra, G.S.; Alderwick, L.J.; Fuetterer, K.
Synthesis of alpha-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and maltokinase Pep2
ACS Chem. Biol.
8
2245-2255
2013
Mycobacterium tuberculosis (O07177), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (O07177)
brenda
Fraga, J.; Maranha, A.; Mendes, V.; Pereira, P.J.; Empadinhas, N.; Macedo-Ribeiro, S.
Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway
Sci. Rep.
5
8026
2015
Mycolicibacterium vanbaalenii (A1TH50), Mycobacterium tuberculosis (O07177), Mycolicibacterium vanbaalenii DSM 7251 (A1TH50), Mycobacterium tuberculosis ATCC 25618 (O07177)
brenda
Kermani, A.; Roy, R.; Gopalasingam, C.; Kocurek, K.; Patel, T.; Alderwick, L.; Besra, G.; Ftterer, K.
Crystal structure of the TreS Pep2 complex, initiating a-glucan synthesis in the GlgE pathway of mycobacteria
J. Biol. Chem.
294
7348-7359
2019
Mycolicibacterium smegmatis (A0R6D9), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 (A0R6D9), Mycolicibacterium smegmatis mc(2)155 (A0R6D9)
brenda