Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Taddei, N.; Modesti, A.; Bucciantini, M.; Stefani, M.; Magherini, F.; Vecchi, M.; Raugei, G.; Ramponi, G.
    Properties of N-terminus truncated and C-terminus mutated muscle acylphosphatases (1995), FEBS Lett., 362, 175-179.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.1.7 Urea R97Q mutant, at low urea concentration, sharp activation with maximum, about 50% activation at 3 M urea, followed by rapid inactivation: 6 M: 80% inhibition, 8 M: 100% inhibition Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.7 cDNA cloning, wild-type and mutated recombinant acylphosphatase, recombinant protein expression in Escherichia coli strain BL21 Homo sapiens
3.6.1.7 synthetic gene coding for human muscle enzyme, expressed in Escherichia coli strain BL21 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.6.1.7 DELTA1-6 deletion mutant N-terminus truncated mutant lacks the first six residues: reduced specific activity and native-like structure Homo sapiens
3.6.1.7 R97Q reduced specific activity, kinetic and structural properties of R97Q mutant indicate possible role of Arg-97 in the stabilisation of the active site correct conformation, most likely via back-bone and side chain interactions with Arg-23, the residue involved in phosphate binding by the enzyme Homo sapiens
3.6.1.7 Y98Q reduced specific activity, kinetic and structural properties of Y98Q mutant indicate possible involvement of Tyr-98 in stabilisation of acylphosphatase overall structure Homo sapiens

General Stability

EC Number General Stability Organism
3.6.1.7 muscular enzyme, sensitive to urea: urea denaturation Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.7 phosphate phosphate, competitive inhibition, muscular isoenzyme, wild-type, Ki: 0.98 mM, R97Q Ki: 1.79 mM, Y98Q Ki: 1.17 mM, DELTA6 deletion mutant Ki: 1.19 mM Homo sapiens
3.6.1.7 Urea reversibel inhibition, wild-type and DELTA6 deletion mutant, 4.2 M: 50% inhibition, Y98Q, 3.8 M: 50% inhibition, R97Q, at low urea concentration sharp activation, maximum activation at 3 M: 50% activation, followed by rapid inactivation, 6 M: 80% inhibition, 8 M 100% inhibition; wild-type and mutants, urea inactivation studies Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 additional information
-
 additional information kinetic studies Homo sapiens
3.6.1.7 0.41
-
 benzoyl phosphate Y98Q Homo sapiens
3.6.1.7 0.51
-
 benzoyl phosphate wild-type, muscle Homo sapiens
3.6.1.7 0.55
-
 benzoyl phosphate DELTA6 deletion mutant Homo sapiens
3.6.1.7 1.14
-
 benzoyl phosphate R97Q Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Homo sapiens
-
 human
-
3.6.1.7 Homo sapiens
-
 two different isoenzymes: skeletal muscle and erythrocyte enzyme
-
3.6.1.7 Homo sapiens
-
 several mutants, wild-type, DELTA6 deletion mutant: lacking residues 1-6 at the N-terminus and mutated, R97Q and Y98Q, recombinant
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.6.1.7 side-chain modification muscular isoenzyme, acetylated at the N-terminus Homo sapiens

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 recombinant wild-type and mutated acylphosphatases Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.6.1.7 an acylphosphate + H2O = a carboxylate + phosphate catalytic mechanism Homo sapiens
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.6.1.7 renaturation after treatment with urea Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 muscle
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.7 2500
-
 DELTA6 deletion mutant Homo sapiens
3.6.1.7 3600
-
 Y98Q Homo sapiens
3.6.1.7 4700
-
 R97Q Homo sapiens
3.6.1.7 7000
-
 wild-type, muscle Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 1,3-diphosphoglycerate + H2O
-
 Homo sapiens 3-phosphoglycerate + phosphate
-
 ?
3.6.1.7 acetyl phosphate + H2O
-
 Homo sapiens acetate + phosphate
-
 ?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens carboxylate + phosphate
-
 ?
3.6.1.7 benzoyl phosphate + H2O
-
 Homo sapiens benzoate + phosphate
-
 ?
3.6.1.7 carbamoyl phosphate + H2O
-
 Homo sapiens carbamate + phosphate
-
 ?
3.6.1.7 additional information specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens ?
-
 ?
3.6.1.7 additional information hydrolyzes phosphorylated intermediate formed during activity of membrane pump ATPase Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 More two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.7 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.7 additional information
-
 muscle enzyme is very basic protein Homo sapiens
3.6.1.7 3.7 4.4 R97Q Homo sapiens
3.6.1.7 4.7 5.9 DELTA6 deletion mutant Homo sapiens
3.6.1.7 4.8 5.8 wild-type, muscle Homo sapiens
3.6.1.7 5 5.9 Y98Q Homo sapiens
3.6.1.7 5.3
-
 assay at Homo sapiens