3.1.8.2: diisopropyl-fluorophosphatase

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For detailed information about diisopropyl-fluorophosphatase, go to the full flat file.

Reaction

Synonyms

DFPase, di-isopropylphosphorofluoridate fluorohydrolase, dialkylfluorophosphatase, diisopropyl fluorophosphatase, diisopropyl phosphorofluoridate hydrolase, diisopropylfluorophosphatase, diisopropylfluorophosphonate dehalogenase, diisopropylphosphofluoridase, EC 3.8.2.1, h-PON1, isopropylphosphorofluoridase, More, OP-hydrolyzing enzyme, OPA anhydrase, OPA anhydrolase, OPAA, OPAA-2, opd, OPH, organophosphate acid anhydrase, organophosphate anhydrolase/prolidase, organophosphorus acid anhydrolase, organophosphorus hydrolase, organophosphorus-hydrolyzing enzyme, paraoxonase 1, phosphotriesterase, PON1, PTES5, RC, regucalcin, senescence marker protein-30, SMP30, somanase, tabunase

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.8 Phosphoric-triester hydrolases

                3.1.8.2 diisopropyl-fluorophosphatase

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Results	in table
22	Activating Compound
13	AA Sequence
29	Application
1	CAS Registry Number
20	Cloned(Commentary)
14	Crystallization (Commentary)
1	Expression
21	General Information
4	General Stability
36	Inhibitors
59	kcat/KM [mM/s]
5	Ki Value [mM]
76	KM Value [mM]
8	Localization
54	Metals/Ions
15	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
86	Organism
49	PDB ID
11	pH Optimum
3	pH Range
1	pH Stability
1	pI Value
2	Posttranslational Modification
86	Protein Variants
23	Purification (Commentary)
16	Reaction
1	Reaction Type
74	Reference
1	Renatured (Commentary)
42	Source Tissue
54	Specific Activity [micromol/min/mg]
4	Storage Stability
247	Substrates and Products (Substrate)
20	Subunits
98	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
54	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 3.1.8.2 - diisopropyl-fluorophosphatase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

glycoprotein

Homo sapiens

-

N-glycosylation at amino acids 13 and 171

670953

side-chain modification

Loligo vulgaris

Q7SIG4

covalent attachment of polyethylene glycol (PEG) chains to enzymes is a prominent solution to overcome these issues. PEGylation enlarges the hydrodynamic radius of proteins and shields its surface. PEG modification increases the stability against proteases, reduces immunogenicity, and delays renal excretion significantly leading to prolonged half-life, reduced side effects, and increased pharmacological efficiency

750923