Heterodimeric aminopeptidase a from bacillus licheniformis NS115

Tae Kwang Oh; Mi Ja Park; Jung Kee Lee; Hyung Kwoun Kim; Hee Sop Nam

doi:10.1271/bbb.61.1934

Heterodimeric aminopeptidase a from bacillus licheniformis NS115

Tae Kwang Oh
, Mi Ja Park
, Jung Kee Lee
, Hyung Kwoun Kim
, Hee Sop Nam

Biotechnology

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

2 Scopus citations

Abstract

An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light suhunit had no catalytic activity against the substrate and apparent K_mvalues of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.

Original language	English
Pages (from-to)	1934-1936
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	61
Issue number	11
DOIs	https://doi.org/10.1271/bbb.61.1934
State	Published - Jan 1997

Keywords

Aminopeptidase A
Bacillus licheniformis
Heterodimer

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10.1271/bbb.61.1934

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title = "Heterodimeric aminopeptidase a from bacillus licheniformis NS115",

abstract = "An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light suhunit had no catalytic activity against the substrate and apparent Kmvalues of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.",

keywords = "Aminopeptidase A, Bacillus licheniformis, Heterodimer",

author = "Oh, \{Tae Kwang\} and Park, \{Mi Ja\} and Lee, \{Jung Kee\} and Kim, \{Hyung Kwoun\} and Nam, \{Hee Sop\}",

year = "1997",

month = jan,

doi = "10.1271/bbb.61.1934",

language = "English",

volume = "61",

pages = "1934--1936",

journal = "Bioscience, Biotechnology and Biochemistry",

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T1 - Heterodimeric aminopeptidase a from bacillus licheniformis NS115

AU - Oh, Tae Kwang

AU - Park, Mi Ja

AU - Lee, Jung Kee

AU - Kim, Hyung Kwoun

AU - Nam, Hee Sop

PY - 1997/1

Y1 - 1997/1

N2 - An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light suhunit had no catalytic activity against the substrate and apparent Kmvalues of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.

AB - An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light suhunit had no catalytic activity against the substrate and apparent Kmvalues of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.

KW - Aminopeptidase A

KW - Bacillus licheniformis

KW - Heterodimer

UR - https://www.scopus.com/pages/publications/0031264421

U2 - 10.1271/bbb.61.1934

DO - 10.1271/bbb.61.1934

M3 - Article

C2 - 9404075

AN - SCOPUS:0031264421

SN - 0916-8451

VL - 61

SP - 1934

EP - 1936

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

IS - 11

ER -

Heterodimeric aminopeptidase a from bacillus licheniformis NS115

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Keywords

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