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Literature summary extracted from

  • Helwig, J.J.; Farooqui, A.A.; Bollack, C.; Mandel, P.
    Purification and some properties of tartrate-sensitive acid phosphatase from rabbit kidney cortex (1978), Biochem. J., 175, 321-329.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.2 F-
-
 Oryctolagus cuniculus
3.1.3.2 formaldehyde
-
 Oryctolagus cuniculus
3.1.3.2 Hg2+ HgCl2 Oryctolagus cuniculus
3.1.3.2 NaH2PO4
-
 Oryctolagus cuniculus
3.1.3.2 Tartrate
-
 Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.2 0.25
-
 4-nitrophenyl phosphate acidic enzyme form Oryctolagus cuniculus
3.1.3.2 1.75
-
 4-nitrophenyl phosphate basic enzyme form Oryctolagus cuniculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.2 64000
-
 x * 64000, SDS-PAGE Oryctolagus cuniculus
3.1.3.2 101000
-
 basic enzyme form, glycerol gradient ultracentrifugation Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.2 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.2 an acid and a basic enzyme form Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.2 kidney cortex Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.2 0.7
-
 acidic enzyme form Oryctolagus cuniculus
3.1.3.2 12
-
 basic enzyme form Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.2 1-naphthyl phosphate + H2O
-
 Oryctolagus cuniculus 1-naphthol + phosphate
-
 ?
3.1.3.2 2,3-diphosphoglycerate + H2O hydrolysed by basic enzyme form, no activity with acidic enzyme form Oryctolagus cuniculus ?
-
 ?
3.1.3.2 4-nitrophenyl phosphate + H2O
-
 Oryctolagus cuniculus 4-nitrophenol + phosphate
-
 ?
3.1.3.2 AMP + H2O
-
 Oryctolagus cuniculus adenosine + phosphate
-
 ?
3.1.3.2 ATP + H2O no activity Oryctolagus cuniculus ADP + phosphate
-
 ?
3.1.3.2 CMP + H2O
-
 Oryctolagus cuniculus cytidine + phosphate
-
 ?
3.1.3.2 D-fructose 1,6-diphosphate + H2O
-
 Oryctolagus cuniculus ?
-
 ?
3.1.3.2 D-ribose 5-phosphate + H2O
-
 Oryctolagus cuniculus D-ribose + phosphate
-
 ?
3.1.3.2 Glucose 6-phosphate + H2O hydrolysed by the basic enzyme form, no hydrolysis by the acidic enzyme form Oryctolagus cuniculus Glucose + phosphate
-
 ?
3.1.3.2 GMP + H2O
-
 Oryctolagus cuniculus guanosine + phosphate
-
 ?
3.1.3.2 phosphopyruvate + H2O
-
 Oryctolagus cuniculus pyruvate + phosphate
-
 ?
3.1.3.2 pyridoxal 5'-phosphate + H2O
-
 Oryctolagus cuniculus pyridoxal + phosphate
-
 ?
3.1.3.2 UMP + H2O
-
 Oryctolagus cuniculus uridine + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.2 ? x * 64000, SDS-PAGE Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.2 55
-
-
 Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.2 3.4 5.4 acidic enzyme form Oryctolagus cuniculus
3.1.3.2 3.8 4.2 basic enzyme form Oryctolagus cuniculus