| Identification | Back Directory | [Name]
AMINOACYLASE | [CAS]
9012-37-7 | [Synonyms]
ACYLASE
ACYLASE 1
ACYLASE I
histozyme
hippurase
acyclase I
Acylase 001
benzamidase
hippuricase
EC 3.5.1.14
EC: 3.5.1.14
EC 3.5.1.(4)
AMINOACYLASE
Acylase
Plexazym? AC
aminoacylasei
ACYLASE AMANO
Acylase genus
L-AMINOACYLASE
PLEXAZYM(R) AC
Aminoacylase 1
FROM HOG KIDNEY
l-aminoacidacylase
ACYLASE HOG KIDNEY
Acylase 1500 Amano
dehydropeptidaseii
aminoaciddeacylase
acylaseifromhogkidney
froM Aspergillus genus
ACYLASE: FROM HOG KIDNEY
Native Porcine Acylase I
AMINOACYLASE, IMMOBILIZED
ACYLASE 1, FROM PIG KIDNEY
Acylase from Aspergilus sp.
ACYLASE, ASPERGILLUS MELLEUS
ACYLASE FROM PENICILLIUM SP.*
Acylase,from Porcine Kidney
Acylase Amano, Aminoacylase
acylase i from porcine kidney
AminoAcylase (Industry grade)
alpha-n-acylaminoacidhydrolase
N-ACYLAMINO ACID AMIDOHYDROLASE
acylase from aspergillus melleus
AcylaseIExPigKidney(E.C.3.5.1.14)
AMINOACYLASE, ASPERGILLUS MELLEUS
N-ACYL-L-AMINO-ACID AMIDOHYDROLASE
ACYLASE I GRADE II FROM HOG KIDNEY
acylase i from aspergillus melleus
Acylase from Aspergilus sp.
Native Aspergillus genus Acylase I
ACYLASE I FROM HOG KIDNEY, ~30 U/MG
ACYLASE I, IMMOBILIZED ON EUPERGIT C
Native Aspergillus melleus Acylase I
ACYLASE I GRADE I FROM PORCINE KIDNEY
acylase from streptomyces chartreusis
acylase from streptomyces toyocaensis
Acylase from porcine kidney, lyophil.
acylase from streptomyces zaomyceticus
acylase from streptomyces hachijoensis
acylase from streptomyces griseocarneus
LYOPHILIZED POWDER,>2000 UNITS/MG PROTEIN
AcylaseIfromporcinekidneylyophilizedpowder
Aminoacylase, immobilized, Plexazym(R) AC
N-acyl-aliphatic-L-amino acid amidohydrolase
ACYLASE I FROM ASPERGILLUS MELLEUS, >0.5 U/MG
ACYLASE FROM STREPTOMYCES HACHIJOENSIS, >30 U/G*
ACYLASE FROM STREPTOMYCES TOYOCAENSIS, ~40 U/G*
ACYLASE FROM STREPTOMYCES CHARTREUSIS, >0.1U/MG*
ACYLASE FROM ASPERGILLUS MELLEUS, 2-5 U/MG*
ACYLASE I FROM HOG KIDNEY, MR ~45300, 70 -110 U/MG
ACYLASE FROM STREPTOMYCES ZAOMYCETICUS, ~0.25 U/MG*
ACYLASE FROM STREPTOMYCES GRISEOCARNEUS, ~0.15 U/MG*
SALT-FREE ,LYOPHILIZED POWDER,500-1500UNITS/MG PROTEIN
ACYLASE I FROM HOG KIDNEY LYOPH. SALT-FR POWDER ~15 U/MG
Acylase I from Aspergillus sp., Immobilized on Eupergit C
Acylase I, immobilized on Eupergit? C from Aspergillus sp.
Acylase I, immobilized on Eupergit(R) C from Aspergillus sp.
Amano Acylase >=30,000 U/g, pH 8.0, 50 C (Optimum pH and temperature)
Acylase I from porcine kidney,Aminoacylase, N-Acylamino acid amidohydrolase | [EINECS(EC#)]
232-732-3 | [Molecular Formula]
NULL | [MDL Number]
MFCD00081285 | [MOL File]
9012-37-7.mol | [Molecular Weight]
537.523 |
| Hazard Information | Back Directory | [Description]
Aminoacylase-1 (EC 3.5.1.14) is a homodimeric zinc-binding metalloenzyme. A cytosolic enzyme with a wide range of tissue expression, it cleaves acylated L-amino acids (except L-aspartate) into L-amino acids and an acyl group. L-aspartate derivatives are cleaved by aminoacylase-2 (aspartoacylase). Aminoacylase-1 is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins. | [Uses]
Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids . | [Application]
Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids. | [Biological Functions]
Aminoacylases (N-acyl-L-amino acid amidohydrolases; EC 3.5.1.14) are widely found in animals, plants and microorganisms. The primary function of these enzymes is to remove acyl residues from N-acetylated amino acids although they may also be capable of hydrolysing carboxylic acid amides to fatty acid anions and L-amino acids. Although the catalytic mechanism of aminoacylases has been known for decades, the physiological role of these enzymes is still poorly understood. Activities of a similar nature, however, have been found in certain carboxypeptidases, aminopeptidases and dipeptidases. It could be therefore suggested that aminoacylases have a role to play in protein/peptide turnover. | [General Description]
Acylase I belongs to the aminoacylase family of enzymes. | [Biological Activity]
Acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. n-Butylmalonic acid is an inhibitor of acylase I. S-alkyl-N-acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents have been found to be good acylase I substrates. | [Biochem/physiol Actions]
Acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. n-Butylmalonic acid is an inhibitor of acylase I. S-alkyl-N-acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents have been found to be good acylase I substrates . | [Enzyme inhibitor]
Aminoacylase is a metallo-enzyme that needs Zinc (Zn2+) as a cofactor to function. The Zinc ions inside of aminoacylase are each coordinated to histidine, glutamate, aspartate, and water. The Zinc ion polarizes the water, facilitating its deprotonation by a nearby basic residue. The negatively charged hydroxide ion is nucleophilic and attacks the electrophilic carbonyl carbon of the substrate's acyl group.The exact mechanism after this point is unknown, with one possibility being that the carbonyl then reforms, breaks the amide bond, and forms the two products. At some point in the mechanism, another water molecule enters and coordinates with Zinc, returning the enzyme to its original state.
The nucleophilic attack by water is the rate-limiting step of aminoacylase's catalytic mechanism. This nucleophilic attack is reversible while the subsequent steps are fast and irreversible. This reaction sequence is an example of Michaelis–Menten kinetics, allowing one to determine KM, Kcat, Vmax, turnover number, and substrate specificity through classic Michaelis-Menten enzyme experiments. The second and third forward steps cause the formation and release of the reaction's products. |
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