Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Activating Compound

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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)

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

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.12 22
-
 assay at room temperature Brugia malayi
3.1.3.12 22
-
 assay at room temperature Mycobacterium tuberculosis
3.1.3.12 22
-
 assay at room temperature Ancylostoma ceylanicum
3.1.3.12 22
-
 assay at room temperature Toxocara canis
3.1.3.12 22
-
 assay at room temperature Stenotrophomonas maltophilia

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.12 7.5
-
 assay at Brugia malayi
3.1.3.12 7.5
-
 assay at Mycobacterium tuberculosis
3.1.3.12 7.5
-
 assay at Ancylostoma ceylanicum
3.1.3.12 7.5
-
 assay at Toxocara canis
3.1.3.12 7.5
-
 assay at Stenotrophomonas maltophilia

General Information

EC Number General Information Comment Organism
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 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
3.1.3.12 metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Brugia malayi
3.1.3.12 metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Mycobacterium tuberculosis
3.1.3.12 metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Ancylostoma ceylanicum
3.1.3.12 metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Toxocara canis
3.1.3.12 metabolism trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB) Stenotrophomonas maltophilia