Literature summary for 3.1.3.12 extracted from

Cross, M.; Lepage, R.; Rajan, S.; Biberacher, S.; Young, N.D.; Kim, B.N.; Coster, M.J.; Gasser, R.B.; Kim, J.S.; Hofmann, A.
Probing function and structure of trehalose-6-phosphate phosphatases from pathogenic organisms suggests distinct molecular groupings (2017), FASEB J., 31, 920-926 .

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Cloned(Commentary)

Cloned (Comment)	Organism
cloning of wild-type and mutant tagged enzyme with an N-terminal fusion peptide (MGSSH6SSGRENLYFQGH), recombinant expression in Escherichia coli	Brugia malayi

Protein Variants

Protein Variants	Comment	Organism
D213N	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	Brugia malayi
D215N	site-directed mutagenesis, the mutant shows about 80% reduced activity compared to the wild-type enzyme	Brugia malayi
D424N	site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme	Brugia malayi
D428N	site-directed mutagenesis, the mutant shows about 85-90% reduced activity compared to the wild-type enzyme	Brugia malayi

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	55% inhibition of the wild-type enzyme at 10 mM, increased inhibitions of the mutant enzymes, mutant D215N is completely inhibited at 10 mM	Brugia malayi

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	-	?

Organism

Organism	UniProt	Comment	Textmining
Brugia malayi	A8NS89	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant tagged enzymes from Escherichia coli by anion exchange and nickel affinity chromatography, the N-terminal His6-fusion peptide is proteolytically removed from the target proteins using tobacco etch virus (TEV) protease	Brugia malayi

Reaction

Reaction	Comment	Organism	Reaction ID
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	Brugia malayi	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	-	?

Synonyms

Synonyms	Comment	Organism
Bm1_08695	-	Brugia malayi
Bmal-TPP	-	Brugia malayi
TPP	-	Brugia malayi
trehalose-6-phosphate phosphatase	-	Brugia malayi

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	-	assay at room temperature	Brugia malayi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Brugia malayi

General Information

General Information	Comment	Organism
evolution	TPP belongs to the superfamily of haloacid dehalogenase (HAD) phosphatases that share a catalytic domain with the topology of a Rossmann fold	Brugia malayi
additional information	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, molecular mechanism, overview. BmTPP structural topology, structure comparisons	Brugia malayi

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Release 2023.1 (January 2023)