Detection of a single, metal-independent aminopeptidase activity in polymyxin-extracts from Escherichia coli B

M. Teuber; G. Cerny

doi:10.1007/BF00408910

Detection of a single, metal-independent aminopeptidase activity in polymyxin-extracts from Escherichia coli B

M. Teuber, G. Cerny

Life Sciences

Technical University of Munich

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

The supernatant of Escherichia coli B autolysed in the presence of polymyxin B contains a single, metal-independent aminopeptidase activity (E.C.-group 3.4.1). The enzyme cleaves the 4-nitroanilides of L-alanine, L-lysine, L-leucine, glycine, and weakly L-phenylalanine. The corresponding N-acetyl-L-alanine-, L-glutamic acid- and L-cysteine-derivatives are not attacked.

Original language	English
Pages (from-to)	235-240
Number of pages	6
Journal	Archiv für Mikrobiologie
Volume	91
Issue number	3
DOIs	https://doi.org/10.1007/BF00408910
State	Published - Sep 1973

Access to Document

10.1007/BF00408910

Cite this

@article{21887aa8d4454b18997aef87841338e0,

title = "Detection of a single, metal-independent aminopeptidase activity in polymyxin-extracts from Escherichia coli B",

abstract = "The supernatant of Escherichia coli B autolysed in the presence of polymyxin B contains a single, metal-independent aminopeptidase activity (E.C.-group 3.4.1). The enzyme cleaves the 4-nitroanilides of L-alanine, L-lysine, L-leucine, glycine, and weakly L-phenylalanine. The corresponding N-acetyl-L-alanine-, L-glutamic acid- and L-cysteine-derivatives are not attacked.",

author = "M. Teuber and G. Cerny",

year = "1973",

month = sep,

doi = "10.1007/BF00408910",

language = "English",

volume = "91",

pages = "235--240",

journal = "Archiv f{\"u}r Mikrobiologie",

issn = "0302-8933",

publisher = "Springer Verlag",

number = "3",

}

TY - JOUR

T1 - Detection of a single, metal-independent aminopeptidase activity in polymyxin-extracts from Escherichia coli B

AU - Teuber, M.

AU - Cerny, G.

PY - 1973/9

Y1 - 1973/9

N2 - The supernatant of Escherichia coli B autolysed in the presence of polymyxin B contains a single, metal-independent aminopeptidase activity (E.C.-group 3.4.1). The enzyme cleaves the 4-nitroanilides of L-alanine, L-lysine, L-leucine, glycine, and weakly L-phenylalanine. The corresponding N-acetyl-L-alanine-, L-glutamic acid- and L-cysteine-derivatives are not attacked.

AB - The supernatant of Escherichia coli B autolysed in the presence of polymyxin B contains a single, metal-independent aminopeptidase activity (E.C.-group 3.4.1). The enzyme cleaves the 4-nitroanilides of L-alanine, L-lysine, L-leucine, glycine, and weakly L-phenylalanine. The corresponding N-acetyl-L-alanine-, L-glutamic acid- and L-cysteine-derivatives are not attacked.

UR - http://www.scopus.com/inward/record.url?scp=0015884874&partnerID=8YFLogxK

U2 - 10.1007/BF00408910

DO - 10.1007/BF00408910

M3 - Article

C2 - 4354503

AN - SCOPUS:0015884874

SN - 0302-8933

VL - 91

SP - 235

EP - 240

JO - Archiv für Mikrobiologie

JF - Archiv für Mikrobiologie

IS - 3

ER -

Detection of a single, metal-independent aminopeptidase activity in polymyxin-extracts from Escherichia coli B

Abstract

Access to Document

Other files and links

Fingerprint

Cite this