Trehalose-phosphatase

Thus, the two substrates of this enzyme are alpha,alpha'-trehalose 6-phosphate and H₂O, whereas its two products are alpha,alpha-trehalose and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is alpha,alpha-trehalose-6-phosphate phosphohydrolase. Other names in common use include trehalose 6-phosphatase, trehalose 6-phosphate phosphatase, and trehalose-6-phosphate phosphohydrolase. This enzyme participates in starch and sucrose metabolism.

References

CABIB E, LELOIR LF (1958). "The biosynthesis of trehalose phosphate". J. Biol. Chem. 231 (1): 259–75. PMID 13538966.
CANDY DJ, KILBY BA (1961). "The biosynthesis of trehalose in the locust fat body". Biochem. J. 78: 531–6. PMC 1205371. PMID 13690400.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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