Aminoacylase

한글명:Aminoacylase

카스 번호9012-37-7

상품명:Aminoacylase

CBNumberCB3458624

분자식C30H34Cl2N4O

포뮬러 무게537.52316

MOL 파일9012-37-7.mol

화학적 성질

저장 조건	2-8°C
물리적 상태	무염, 동결건조 분말
색상	옐로우 브라운 컬러
EPA	Aminoacylase (9012-37-7)

위험 및 안전 성명

위험품 표기	Xn
위험 카페고리 넘버	36/37/38-42
안전지침서	22-24/25-36/37-26-24
WGK 독일	3
RTECS 번호	BF4890000
F 고인화성물질	3-10-21
HS 번호	35079090

그림문자(GHS)

Aminoacylase 화학적 특성, 용도, 생산

개요
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.
용도
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 .
주요 응용
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.
일반 설명
Acylase I belongs to the aminoacylase family of enzymes.
효소 저해제
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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