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新型β-内酰胺化合物PS-5的去乙酰化作用。III. 假单胞菌属1158中L-氨基酸酰基转移酶和D-氨基酸酰基转移酶的酶学特性

Deacetylation of PS-5, a new beta-lactam compound. III. Enzymological characterization of L-amino acid acylase and D-amino acid acylase from Pseudomonas sp. 1158.

作者信息

Kubo K, Ishikura T, Fukagawa Y

出版信息

J Antibiot (Tokyo). 1980 Jun;33(6):556-65. doi: 10.7164/antibiotics.33.556.

DOI:10.7164/antibiotics.33.556
PMID:7419469
Abstract

L-Amino acid acylase and D-amino acid acylase were stable below 50 degrees C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30 degrees C they showed the highest reaction velocity in phosphate buffer of pH 7.4. Hg++ and Cu++ severely inactivated their activity. Activation by Co++ was observed on L-amino acid acylase, but not on D-amino acid acylase. p-Chloromercuribenzoate inhibited both enzymes, whereas ethylenediamine tetraacetate was very inhibitory on L-amino acid acylase only. With N-acetyl- and N-chloroacetyl-amino acids as substrates, they were relatively stereo-specific. They acted as a peptidase on dipeptides and tripeptides. Although N-acetylglycine was attacked by the two enzymes, N-acetylglucosamine and N-acetylethanolamine were insusceptible. PS-5 was converted to NS-5 (deacetyl PS-5) by L-amino acid acylase as well as by D-amino acid acylase.

摘要

L-氨基酸酰化酶和D-氨基酸酰化酶在50摄氏度以下是稳定的,尽管在较高温度下D-酶比L-酶更耐热。在30摄氏度时,它们在pH 7.4的磷酸盐缓冲液中表现出最高的反应速度。Hg++和Cu++会严重使其活性失活。观察到Co++对L-氨基酸酰化酶有激活作用,但对D-氨基酸酰化酶没有激活作用。对氯汞苯甲酸抑制这两种酶,而乙二胺四乙酸仅对L-氨基酸酰化酶有很强的抑制作用。以N-乙酰基和N-氯乙酰基氨基酸为底物时,它们具有相对的立体特异性。它们对二肽和三肽起肽酶的作用。尽管N-乙酰甘氨酸会被这两种酶作用,但N-乙酰葡糖胺和N-乙酰乙醇胺不受影响。L-氨基酸酰化酶和D-氨基酸酰化酶都能将PS-5转化为NS-5(脱乙酰基PS-5)。

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Deacetylation of PS-5, a new beta-lactam compound. III. Enzymological characterization of L-amino acid acylase and D-amino acid acylase from Pseudomonas sp. 1158.新型β-内酰胺化合物PS-5的去乙酰化作用。III. 假单胞菌属1158中L-氨基酸酰基转移酶和D-氨基酸酰基转移酶的酶学特性
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引用本文的文献

1
Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1.从粪产碱杆菌 DA1 中纯化和鉴定 d- 氨基酰化酶。
Appl Environ Microbiol. 1991 Apr;57(4):1259-60. doi: 10.1128/aem.57.4.1259-1260.1991.
2
Production and Purification of d-Aminoacylase from Alcaligenes denitrificans and Taxonomic Study of the Strain.从脱硝副球菌中生产和纯化 d- 氨基酰化酶及菌株的分类学研究。
Appl Environ Microbiol. 1988 Apr;54(4):984-9. doi: 10.1128/aem.54.4.984-989.1988.
3
Structural-based mutational analysis of D-aminoacylase from Alcaligenes faecalis DA1.
粪产碱杆菌DA1来源的D-氨基酸酰化酶基于结构的突变分析
Protein Sci. 2002 Nov;11(11):2545-50. doi: 10.1110/ps.0220902.