Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
AtTPS1
-
functional synthase and phosphatases in vivo
AtTPS10
-
belongs to the class II proteins
AtTPS11
-
belongs to the class II proteins
AtTPS5
-
belongs to the class II proteins
AtTPS7
-
belongs to the class II proteins
AtTPS8
-
belongs to the class II proteins
AtTPS9
-
belongs to the class II proteins
chromosomal trehalose 6-phosphate phosphatase
-
ChTPSP
-
bifunctional enzyme
extrachromosomal trehalose 6-phosphate phosphatase
trehalose 6-P phosphatase
-
-
trehalose 6-phosphatase
-
-
-
-
trehalose 6-phosphate phosphatase
trehalose phosphate phosphatase
-
-
-
-
trehalose-6-P phosphatase
trehalose-6-phophate synthase/phosphatase
trehalose-6-phosphate phosphatase
trehalose-6-phosphate phosphatase-related protein
trehalose-6-phosphate synthase/phosphatase
trehalose-6P phosphatase
-
-
trehalose-P phosphatase
-
-
trehalose-phosphate phosphatase
trehalose-phosphate phosphatase 7
UniProt
AtTPS6
-
belongs to the class II proteins
AtTPS6
-
encodes a class II trehalose-6-phosphate synthase that contains both synthase and phophatase domains
chTPP
-
ecTPP
-
extrachromosomal trehalose 6-phosphate phosphatase
-
extrachromosomal trehalose 6-phosphate phosphatase
-
-
GOB-1
-
HMPREF3289_15950
-
MtbTPP
-
Mtub-TPP
-
OrlA
-
-
OsTPP1
-
-
OtsB
-
otsB2
-
Paer-chTPP
-
Rv3372
-
RW109_RW109_00128
locus name
RW109_RW109_00128
locus name
-
T6P phosphatase
-
T6PP
-
-
TPP
-
-
-
-
Tpp1
-
TPPA
-
-
TPPB
-
-
TPS2
-
TPSP
-
TPSP
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
TPSP
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
-
TPSP
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
-
trehalose 6-phosphate phosphatase
-
-
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
-
trehalose 6-phosphate phosphatase
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
-
trehalose 6-phosphate phosphatase
-
trehalose 6-phosphate phosphatase
-
trehalose 6-phosphate phosphatase
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose 6-phosphate phosphatase
-
-
trehalose-6-P phosphatase
-
-
trehalose-6-P phosphatase
-
trehalose-6-phophate synthase/phosphatase
-
-
trehalose-6-phophate synthase/phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase
-
trehalose-6-phosphate phosphatase
-
-
trehalose-6-phosphate phosphatase-related protein
-
-
trehalose-6-phosphate phosphatase-related protein
-
-
-
trehalose-6-phosphate synthase/phosphatase
-
trehalose-6-phosphate synthase/phosphatase
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
trehalose-6-phosphate synthase/phosphatase
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
-
trehalose-6-phosphate synthase/phosphatase
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
-
trehalose-phosphate phosphatase
-
-
trehalose-phosphate phosphatase
-
trehalose-phosphate phosphatase
-
-
additional information
Bm-TPP is a member of the HAD-like hydrolase super family II based on the conserved motifs required for catalytic reaction
additional information
-
the enzyme belongs to the HAD-like hydrolase superfamily
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
-
-
-
-
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
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
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
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
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
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
molecular mechanism, overview. The catalytic mechanism involves a nucleophilic attack by an aspartate in the active site targeting the phosphorus of the phosphate group, which undergoes a conformational change via a trigonal bipyramidal transition state. The release of trehalose renders an enzyme-phosphate conjugate that is hydrolyzed in a second step. It is generally believed that a water molecule is activated by a second aspartate to form a hydroxyl ion that performs a nucleophilic attack on the phosphorus, thus hydrolyzing the aspartate-phosphoester and release of the phosphate. In contrast to Asp213, the residue inferred to carry out the nucleophilic attack on the substrate, Asp215 and Asp428 of enzyme BmTPP are involved in the chemistry steps of enzymatic hydrolysis of the substrate
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
-
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-mannose 6-phosphate + H2O
D-mannose + phosphate
-
16% of the activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
trehalose 6-phosphate + H2O
trehalose + phosphate
trehalose-6-phosphate + H2O
trehalose + phosphate
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
additional information
?
-
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
16% of the activity with trehalose 6-phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
3.1% of activity with trehalose 6-phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
3.1% of activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
-
7% of the activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
-
activated by trehalose
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
bioinformatical approach, coexpression networks analyzed
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
high substrate specificity, overview
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
pleiotropic defective phenotype of disrupted TPS2, cell wall integrity and ability to form chlamydospores maintained, reduced growth and temperature sensitivity (42°C) of homozygous mutant, severe oxidative exposure (50 mM H2O2), null mutants reveal adaptive antioxidant response and cross-tolerance between temperature and oxidative stress, expression of TPS2 and TPS1 genes promoted in wild-type cells in response to acute (50 mM) but not gentle (5 mM) oxidative exposure
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
protective role of the trehalose biosynthetic pathway in the cellular response to oxidative stress and subsequently in the resistance to phagocytosis
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the product trehalose acts as a global against abiotic stress
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the enzyme is absolutely specific for trehalose 6-phosphate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
glucose disaccharide with alpha,alpha-1,1 linkage
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the enzyme is involved in trehalose biosynthesis, trehalose serves as a stress protectant and/or reserve carbohydrate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
high substrate specificity of recombinant enzyme
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
3.1.3.12 trehalose-phosphatase
more
top
