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Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes. Acy1 recombinant human produced in e. coli is a single, non-... SDS-PAGE. ACY1. Mole weight: 48 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. N-acyl-L-amino-acid amidohydrolase; ACY-1, ACY1D; ACYLASE; ACY1; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short
AminoAcylase (Industry grade)
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. Purity: 0.98. ACY1. Storage: at -4-25°C, dry, dark conditions for 3 years. Form: Lyophilized powder. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1620.
glutaryl-7-aminocephalosporanic-acid acylase
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C. Group: Enzymes. Synonyms: 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase. Enzyme Commission Number: EC 3.5.1.93. CAS No. 56645-46-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4485; glutaryl-7-aminocephalosporanic-acid acylase; EC 3.5.1.93; 56645-46-6; 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase. Cat No: EXWM-4485.
L-Aminoacylase (Crude Enzyme)
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Pack: 100ml. Cat No: NATE-1835.
6-Aminopenicillanic acid
6-Aminopenicillanic acid (6-APA) is an important precursor for the synthesis of b-lactam antibiotics. 6-Aminopenicillanic acid is the main product of Penicillin G (PenG) hydrolyzed by penicillin acylase (PA) [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 6-APA. CAS No. 551-16-6. Pack Sizes: 500 mg. Product ID: HY-W013549.
6-Aminopenicillanic acid
6-Aminopenicillanic acid (6-APA) is an important precursor for the synthesis of lactam antibiotics. 6-Aminopenicillanic acid is the main product of Penicillin G (PenG) hydrolyzed by penicillin acylase (PA). Group: Inhibitors. Alternative Names: (25,5R,6R)-6-AMINO-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC ACID;(2S,5R,6R)-6-AMINO-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO-[3.2.0]HEPTANE-2-CARBOXYLIC ACID;6-AMINO-2,2-DIMETHYL-5-OXOPERHYDROAZETO[2,1-B][1,3]THIAZOLE-3-CARBOXYLIC ACID;6-AMINO-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC ACID;6-APA;(+)-6-AMINOPENICILLANIC ACID;6-AMINOPENICILLANIC ACID;6-AMINO PENICILLINIC ACID. CAS No. 551-16-6. Molecular formula: C8H12N2O3S. Mole weight: 216.26. Appearance: Solid. Purity: ≥98.0%. Canonical SMILES: [C@H]12SC ([C@@H] (N1C (=O)[C@H]2N)C (=O)O) (C)C. Catalog: ACM551166.
7-Bromoacetyl aminocephalosporanic Acid
An analog of glutaryl-7-amino cephalosporanic acid (GL-7-ACA). Can inhibit and specifically alkylate GL-7-ACA acylase (C130) from Pseudomonas sp.130 by forming a carbon-carbon bond between BA-7-ACA and the C-2 on indole ring of Trp- β4 residue of C130. Group: Biochemicals. Alternative Names: (6R-trans)-3-[(Acetyloxy)methyl]-7-[(bromoacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic Acid; 7- (2-Bromoacetamido) cephalosporanic Acid. Grades: Highly Purified. CAS No. 26973-80-8. Pack Sizes: 100mg. US Biological Life Sciences.
Worldwide
Acylase I from Aspergillus sp., Immobilized on Eupergit C
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 50 U/g moist material. Storage: 2-8°C. Source: Aspergillus sp. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0030.
amidase
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation. Group: Enzymes. Synonyms: acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Enzyme Commission Number: EC 3.5.1.4. CAS No. 9012-56-0. Amidase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4428; amidase; EC 3.5.1.4; 9012-56-0; acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous). Cat No: EXWM-4428.
aspartoacylase
Aspartoacylase (EC 3.5.1.15, aminoacylase II, N-acetylaspartate amidohydrolase, acetyl-aspartic deaminase, acylase II, ASPA) is a hydrolase enzyme responsible for catalyzing the deacylation of N-acetyl-l-aspartate (N-acetylaspartate,NAA) into aspartate and acetate. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the brain, where it controls the levels of N-actetyl-l-aspartate. Group: Enzymes. Synonyms: aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Enzyme Commission Number: EC 3.5.1.15. CAS No. 9031-86-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4404; aspartoacylase; EC 3.5.1.15; 9031-86-1; aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II. Cat No: EXWM-4404.
Cefathiamidine Impurity 1
An analog of glutaryl-7-amino cephalosporanic acid (GL-7-ACA). Can inhibit and specifically alkylate GL-7-ACA acylase (C130) from Pseudomonas sp.130 by forming a carbon-carbon bond between BA-7-ACA and the C-2 on indole ring of Trp-β4 residue of C130. Synonyms: (6R-trans)-3-[(Acetyloxy)methyl]-7-[(bromoacetyl)amino]-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic Acid; 7-(2-Bromoacetamido)cephalosporanic Acid. Grades: > 95%. CAS No. 26973-80-8. Molecular formula: C12H13BrN2O6S. Mole weight: 393.22.
DL-Glutamic Acid Monohydrate (DL-Glu-OH), 99+%
Glutamic acid is a non-essential amino acid that is also an excitatory amino acid (EAA) because of its role in neurotransmission.1 Its name derives from its historical isolation from wheat gluten. A detailed review of the chemistry of glutamic acid has been published. 2DL-Glutamic acid has been used as an energy source in the isolation of cultured Thiobacillus acidophilus.3 It has been utilized as a supplement in the diet of chicks and been shown to lead to grown depression.4 DL-Glutamic acid has been utilized as a nitrogen source for the culture of nematode eggs from Arkansas Fungus 18 (ARF18) and Pochonia chlamydospora var. chlamydospora.5A method for the analysis of DL-glutamic acid and other amino acids via copper(II) ion, hydrogen peroxide, and pyrocathechol violet has been published.6 The resolution of DL-glutamic acid as its acetyl derivative through the use of porcine renal acylase I has been reported.2DLGlutamic acid has been used as a starting material for the synthesis of imidazo[1,5-a]quinoxaline amides and carbamates that bind with high affinity to the GABAA/benzodiazepine receptor in culturedSf 9 cells.7. Group: Biochemicals. Alternative Names: DL-Glu-OH·H2O; (RS)-2-Aminopentanedioic acid monohydrate; DL-glutaminic acid, DL-α-aminoglutaric acid; DL-1-aminopropane-1,3-dicarboxylic acid. Grades: Highly Purified. CAS No. 19285-83-7. Pack Sizes: 100g, 500g, 1Kg. Molecular Formula: C5H9NO4 H2O, Molecular Weight: 165.15. US Biological Life Sciences.
Worldwide
N-acyl-aliphatic-L-amino acid amidohydrolase
Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-α-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoa. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4403; N-acyl-aliphatic-L-amino acid amidohydrolase; EC 3.5.1.14; 9012-37-7; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase. Cat No: EXWM-4403.
Native Aspergillus genus Acylase I
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. CAS No. 9012-37-7. ACY1. Storage: 0-10°C. Source: Aspergillus genus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-1593.
Native Aspergillus melleus Acylase I
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Enzyme activity: the optimum temperature is 40-45 oc, the optimum ph is 8.0 (stable form ph 6-10). the enzyme is activated by cocl2 in the range of 10-4 to 10-3 m. Group: Enzymes. Synonyms: aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; . Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: >0.5 units/mg. Storage: 2-8°C. Form: powder. Source: Aspergillus melleus. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0029.
Native Escherichia coli Penicillin Amidase
The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate. Penicillin amidase is a periplasmic 80k heterodimer with a and b chains (209 and 566 amino acids, respectively). it is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. among all the sources, the enzyme produced by e. coli is most well-characterized and common for industrial application. Applications: Penicillin...; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin Amidase. Mole weight: Mr ~70 kDa. Activity: Type I, 5-10 units/mg protein; Type II, > 10 units/mg protein (E1%/280). Storage: 2-8°C. Form: Type II, ammonium sulfate suspension, Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate. Source: Escherichia coli. penicillin amidase; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Cat No: NATE-0541.
Native Porcine Acylase I
In enzymology, an aminoacylase (EC 3.5.1.14) is an enzyme that catalyzes the chemical reaction:N-acyl-L-amino acid + H2O<-> carboxylate + L-amino acid. Thus, the two substRates of this enzyme are N-acyl-L-amino acid and H2O, whereas its two products are carboxylate and L-amino acid. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme participates in urea cycle and metabolism of amino groups. Protein determined by biuret. Applications: 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 carb...ort acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Enzyme Commission Number: EC 3.5.1.14. CAS No. 9012-37-7. ACY1. Activity: > 2,000 units/mg protein; 500-1,500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Porcine kidney. Species: Porcine. aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14; 9012-37-7. Cat No: NATE-0031.
Penicillin amidase, E. coli
Penicillin amidase (EC 3.5.1.11) (Penicillin acylase) is an enzyme that cleaves the acyl side chains of penicillins. Penicillin amidase can be used for the production of 6-aminopenicillanic acid. Penicillin amidase can also be used in the resolution of racemic mixtures, peptide synthesis, and synthesis of semi-synthetic β-lactam antibiotics [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PGA. CAS No. 9014-6-6. Pack Sizes: 100 mg; 250 mg. Product ID: HY-P2834.
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