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Literature summary for 3.1.3.12 extracted from

  • Cross, M.; Rajan, S.; Chekaiban, J.; Saunders, J.; Hamilton, C.; Kim, J.S.; Coster, M.J.; Gasser, R.B.; Hofmann, A.
    Enzyme characteristics of pathogen-specific trehalose-6-phosphate phosphatases (2017), Sci. Rep., 7, 2015 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.12

Activating Compound

Activating Compound Comment Organism Structure
additional information no notable effects of EDTA Brugia malayi
additional information no notable effects of EDTA Mycobacterium tuberculosis
additional information no notable effects of EDTA Ancylostoma ceylanicum
o-vanadate slight activation Stenotrophomonas maltophilia
sulfate slight activation Stenotrophomonas maltophilia

Inhibitors

Inhibitors Comment Organism Structure
EDTA abolished enzymatic activity of enzyme Smal-TPP in the presence of 1 mM EDTA Stenotrophomonas maltophilia
fluoride
-
 Brugia malayi
molybdate
-
 Brugia malayi
additional information no notable effects of EDTA, no product inhibition, poor effects by sulfate and o-vanadate Ancylostoma ceylanicum
additional information no notable effects of EDTA, no product inhibition Brugia malayi
additional information no notable effects of EDTA, no product inhibition, poor effects by sulfate and o-vanadate Mycobacterium tuberculosis
additional information no product inhibition Stenotrophomonas maltophilia
additional information no product inhibition, no or poor effects by sulfate, EDTA, and o-vanadate Toxocara canis
o-vanadate slight inhibition Brugia malayi
sulfate slight inhibition Brugia malayi

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of trehalose-6-phosphate hydrolysis reveal that the enzyme displays a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, pre-steady state parameters, overview Brugia malayi
additional information
-
 additional information kinetics of trehalose-6-phosphate hydrolysis reveal that the enzyme displays a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, pre-steady state parameters, overview Mycobacterium tuberculosis
additional information
-
 additional information kinetics of trehalose-6-phosphate hydrolysis reveal that the enzyme displays a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, pre-steady state parameters, overview Ancylostoma ceylanicum
additional information
-
 additional information kinetics of trehalose-6-phosphate hydrolysis reveal that the enzyme displays a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, pre-steady state parameters, overview Toxocara canis
additional information
-
 additional information kinetics of trehalose-6-phosphate hydrolysis reveal that the enzyme displays a burst-like kinetic behaviour which is characterised by a decrease of the enzymatic rate after the pre-steady state, pre-steady state parameters, overview Stenotrophomonas maltophilia

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha,alpha-trehalose 6-phosphate + H2O Brugia malayi
-
 alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O Mycobacterium tuberculosis
-
 alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O Ancylostoma ceylanicum
-
 alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O Toxocara canis
-
 alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O Stenotrophomonas maltophilia
-
 alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O Mycobacterium tuberculosis H37Rv
-
 alpha,alpha-trehalose + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Ancylostoma ceylanicum A0A016VAH2
-
-
Brugia malayi A8NS89
-
-
Mycobacterium tuberculosis P9WFZ5
-
-
Mycobacterium tuberculosis H37Rv P9WFZ5
-
-
Stenotrophomonas maltophilia A0A1S2B2X3
-
-
Toxocara canis A0A0B2V3X6
-
-

Reaction

Reaction Comment Organism Reaction ID
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate in the first step, trehalose-6-phosphate binds to the open form of the enzyme, and it is assumed that the occurrence of productive interactions between enzyme and substrate cause the cap domain to rotate towards the core domain (step 2), thus forming a closed substrate-bound form. Nucleophilic attack by an active site aspartate side chain in the third step leads to a covalent intermediate that is further hydrolysed into the two product molecules (step 4). Finally, the enzyme is required to remove the cap from the core domain in a conformational change (step 5). It can reasonably be assumed that the steps involving domain movements (steps 2 and 5) proceed much slower than the chemistry steps (3 and 4). These multiple processes occur in a population of enzyme molecules in a non-synchronised fashion. Additionally, it is possible that individual enzyme molecules undergo a conformational change between open and closed states in the absence of substrate molecules. Such non-synchronised conformational changes will lead to a decrease in the overall rate of the enzymatic reaction of a population of molecules Brugia malayi
a
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate in the first step, trehalose-6-phosphate binds to the open form of the enzyme, and it is assumed that the occurrence of productive interactions between enzyme and substrate cause the cap domain to rotate towards the core domain (step 2), thus forming a closed substrate-bound form. Nucleophilic attack by an active site aspartate side chain in the third step leads to a covalent intermediate that is further hydrolysed into the two product molecules (step 4). Finally, the enzyme is required to remove the cap from the core domain in a conformational change (step 5). It can reasonably be assumed that the steps involving domain movements (steps 2 and 5) proceed much slower than the chemistry steps (3 and 4). These multiple processes occur in a population of enzyme molecules in a non-synchronised fashion. Additionally, it is possible that individual enzyme molecules undergo a conformational change between open and closed states in the absence of substrate molecules. Such non-synchronised conformational changes will lead to a decrease in the overall rate of the enzymatic reaction of a population of molecules Mycobacterium tuberculosis
a
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate in the first step, trehalose-6-phosphate binds to the open form of the enzyme, and it is assumed that the occurrence of productive interactions between enzyme and substrate cause the cap domain to rotate towards the core domain (step 2), thus forming a closed substrate-bound form. Nucleophilic attack by an active site aspartate side chain in the third step leads to a covalent intermediate that is further hydrolysed into the two product molecules (step 4). Finally, the enzyme is required to remove the cap from the core domain in a conformational change (step 5). It can reasonably be assumed that the steps involving domain movements (steps 2 and 5) proceed much slower than the chemistry steps (3 and 4). These multiple processes occur in a population of enzyme molecules in a non-synchronised fashion. Additionally, it is possible that individual enzyme molecules undergo a conformational change between open and closed states in the absence of substrate molecules. Such non-synchronised conformational changes will lead to a decrease in the overall rate of the enzymatic reaction of a population of molecules Ancylostoma ceylanicum
a
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate in the first step, trehalose-6-phosphate binds to the open form of the enzyme, and it is assumed that the occurrence of productive interactions between enzyme and substrate cause the cap domain to rotate towards the core domain (step 2), thus forming a closed substrate-bound form. Nucleophilic attack by an active site aspartate side chain in the third step leads to a covalent intermediate that is further hydrolysed into the two product molecules (step 4). Finally, the enzyme is required to remove the cap from the core domain in a conformational change (step 5). It can reasonably be assumed that the steps involving domain movements (steps 2 and 5) proceed much slower than the chemistry steps (3 and 4). These multiple processes occur in a population of enzyme molecules in a non-synchronised fashion. Additionally, it is possible that individual enzyme molecules undergo a conformational change between open and closed states in the absence of substrate molecules. Such non-synchronised conformational changes will lead to a decrease in the overall rate of the enzymatic reaction of a population of molecules Toxocara canis
a
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate in the first step, trehalose-6-phosphate binds to the open form of the enzyme, and it is assumed that the occurrence of productive interactions between enzyme and substrate cause the cap domain to rotate towards the core domain (step 2), thus forming a closed substrate-bound form. Nucleophilic attack by an active site aspartate side chain in the third step leads to a covalent intermediate that is further hydrolysed into the two product molecules (step 4). Finally, the enzyme is required to remove the cap from the core domain in a conformational change (step 5). It can reasonably be assumed that the steps involving domain movements (steps 2 and 5) proceed much slower than the chemistry steps (3 and 4). These multiple processes occur in a population of enzyme molecules in a non-synchronised fashion. Additionally, it is possible that individual enzyme molecules undergo a conformational change between open and closed states in the absence of substrate molecules. Such non-synchronised conformational changes will lead to a decrease in the overall rate of the enzymatic reaction of a population of molecules Stenotrophomonas maltophilia
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha,alpha-trehalose 6-phosphate + H2O
-
 Brugia malayi alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O
-
 Mycobacterium tuberculosis alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O
-
 Ancylostoma ceylanicum alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O
-
 Toxocara canis alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O
-
 Stenotrophomonas maltophilia alpha,alpha-trehalose + phosphate
-
 ?
alpha,alpha-trehalose 6-phosphate + H2O
-
 Mycobacterium tuberculosis H37Rv alpha,alpha-trehalose + phosphate
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Brugia malayi ?
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Mycobacterium tuberculosis ?
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Ancylostoma ceylanicum ?
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Toxocara canis ?
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Stenotrophomonas maltophilia ?
-
 ?
additional information phosphomolybdate/malachite green phosphate detection method Mycobacterium tuberculosis H37Rv ?
-
 ?

Synonyms

Synonyms Comment Organism
Acey-TPP
-
 Ancylostoma ceylanicum
Bm1_08695
-
 Brugia malayi
Bmal-TPP
-
 Brugia malayi
Mtub-TPP
-
 Mycobacterium tuberculosis
otsB2
-
 Mycobacterium tuberculosis
Rv3372
-
 Mycobacterium tuberculosis
Smal-TPP
-
 Stenotrophomonas maltophilia
TPP
-
 Brugia malayi
TPP
-
 Mycobacterium tuberculosis
TPP
-
 Ancylostoma ceylanicum
TPP
-
 Toxocara canis
TPP
-
 Stenotrophomonas maltophilia
trehalose-6-phosphate phosphatase
-
 Brugia malayi
trehalose-6-phosphate phosphatase
-
 Mycobacterium tuberculosis
trehalose-6-phosphate phosphatase
-
 Ancylostoma ceylanicum
trehalose-6-phosphate phosphatase
-
 Toxocara canis
trehalose-6-phosphate phosphatase
-
 Stenotrophomonas maltophilia

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Brugia malayi
22
-
 assay at room temperature Mycobacterium tuberculosis
22
-
 assay at room temperature Ancylostoma ceylanicum
22
-
 assay at room temperature Toxocara canis
22
-
 assay at room temperature Stenotrophomonas maltophilia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Brugia malayi
7.5
-
 assay at Mycobacterium tuberculosis
7.5
-
 assay at Ancylostoma ceylanicum
7.5
-
 assay at Toxocara canis
7.5
-
 assay at Stenotrophomonas maltophilia

General Information

General Information Comment Organism
evolution the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea Brugia malayi
evolution the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea Mycobacterium tuberculosis
evolution the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea Ancylostoma ceylanicum
evolution the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea Toxocara canis
evolution the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea Stenotrophomonas maltophilia
metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Brugia malayi
metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Mycobacterium tuberculosis
metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Ancylostoma ceylanicum
metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Toxocara canis
metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Stenotrophomonas maltophilia