difructose-anhydride synthase | |||||||||
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Identifiers | |||||||||
EC no. | 3.2.1.134 | ||||||||
CAS no. | 121479-55-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a difructose-anhydride synthase (EC 3.2.1.134) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are bis-D-fructose 2',1:2,1'-dianhydride and H2O, whereas its product is inulobiose.
This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is bis-D-fructose 2',1:2,1'-dianhydride fructohydrolase. This enzyme is also called inulobiose hydrolase.
Hydrolase is a class of enzymes that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.
Aspergillus fumigatus is a species of fungus in the genus Aspergillus, and is one of the most common Aspergillus species to cause disease in individuals with an immunodeficiency.
Aspergillus is a genus consisting of several hundred mould species found in various climates worldwide.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
Gliotoxin is a sulfur-containing mycotoxin that belongs to a class of naturally occurring 2,5-diketopiperazines produced by several species of fungi, especially those of marine origin. It is the most prominent member of the epipolythiopiperazines, a large class of natural products featuring a diketopiperazine with di- or polysulfide linkage. These highly bioactive compounds have been the subject of numerous studies aimed at new therapeutics. Gliotoxin was originally isolated from Gliocladium fimbriatum, and was named accordingly. It is an epipolythiodioxopiperazine metabolite that is one of the most abundantly produced metabolites in human invasive Aspergillosis (IA).
The enzyme inulin fructotransferase (DFA-I-forming) catalyzes the following process:
The enzyme levan fructotransferase (DFA-IV-forming) catalyzes the following process:
In enzymology, an adenylylsulfatase is an enzyme that catalyzes the chemical reaction
In enzymology, an ADP-sugar diphosphatase (EC 3.6.1.21) is an enzyme that catalyzes the chemical reaction
In enzymology, a bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, a bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) (EC 3.6.1.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a bis(5'-nucleosyl)-tetraphosphatase (symmetrical) (EC 3.6.1.41) is an enzyme that catalyzes the chemical reaction
In enzymology, a trimetaphosphatase (EC 3.6.1.2) is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-sugar diphosphatase (EC 3.6.1.45) is an enzyme that catalyzes the chemical reaction
In enzymology, an undecaprenyl-diphosphatase (EC 3.6.1.27) is an enzyme that catalyzes the chemical reaction
The enzyme fructose-2,6-bisphosphate 6-phosphatase (EC 3.1.3.54) catalyzes the reaction
The enzyme mannitol-1-phosphatase (EC 3.1.3.22) catalyzes the reaction
In enzymology, a glycyrrhizinate β-glucuronidase (EC 3.2.1.128) is an enzyme that catalyzes the chemical reaction
Inulinase is an enzyme with systematic name 1-β-D-fructan fructanohydrolase. It catalyses the reaction
Rhamnogalacturonan hydrolase is an enzyme with systematic name rhamnogalacturonan alpha-D-GalA-(1->2)-alpha-L-Rha hydrolase. This enzyme catalyses the following chemical reaction