Substrate variety of a non-metal dependent tagatose-6-phosphate isomerase from Staphylococcus aureus

Deok Kun Oh; Eun Soo Ji; Young Deok Kwon; Hye Jung Kim; Pil Kim

Substrate variety of a non-metal dependent tagatose-6-phosphate isomerase from Staphylococcus aureus

Deok Kun Oh
, Eun Soo Ji
, Young Deok Kwon
, Hye Jung Kim
, Pil Kim

Dept. of Biotechnology

Sejong University
The Catholic University of Korea

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

1 Scopus citations

Abstract

To investigate the substrate variety of a putative non-metal dependent isomerase, the tagatose-6-phosphate isomerase (E.C. 5.3.1.26) structural genes (lacB; 510bp and lacA; 430bp) of Staphylococcus aureus were subcloned and co-expressed. Based on the substrate configuration, various aldoses were surveyed for substrate of ketose isomerization. Among the 10 aldoses tested, D-ribose and D-allose were isomerized by the enzyme. The subunit A and B showed more than 95% activity for D-ribose and 75% for D-allose in the presence of 1mM EDTA compared with non-EDTA conditions, which implying tagatose-6-phosphate isomerase is a non-metal dependent isomerase. Each of subunit A or subunit B alone showed no activity for any of the substrates tested. The affinity constant (K_m) of tagatose-6-phosphate isomerase against D-ribose and D-allose were 26 mM and 142 mM, respectively.

Original language	English
Pages (from-to)	106-111
Number of pages	6
Journal	Microbiology and Biotechnology Letters
Volume	33
Issue number	2
State	Published - Jun 2005

Keywords

Non-metal dependent isomerase
Staphylococcus aureus
Substrate variety
Tagatose-6-phosphate isomerase

Cite this

@article{f239bdf6b34e446cb77f09be6512f668,

title = "Substrate variety of a non-metal dependent tagatose-6-phosphate isomerase from Staphylococcus aureus",

abstract = "To investigate the substrate variety of a putative non-metal dependent isomerase, the tagatose-6-phosphate isomerase (E.C. 5.3.1.26) structural genes (lacB; 510bp and lacA; 430bp) of Staphylococcus aureus were subcloned and co-expressed. Based on the substrate configuration, various aldoses were surveyed for substrate of ketose isomerization. Among the 10 aldoses tested, D-ribose and D-allose were isomerized by the enzyme. The subunit A and B showed more than 95\% activity for D-ribose and 75\% for D-allose in the presence of 1mM EDTA compared with non-EDTA conditions, which implying tagatose-6-phosphate isomerase is a non-metal dependent isomerase. Each of subunit A or subunit B alone showed no activity for any of the substrates tested. The affinity constant (Km) of tagatose-6-phosphate isomerase against D-ribose and D-allose were 26 mM and 142 mM, respectively.",

keywords = "Non-metal dependent isomerase, Staphylococcus aureus, Substrate variety, Tagatose-6-phosphate isomerase",

author = "Oh, \{Deok Kun\} and Ji, \{Eun Soo\} and Kwon, \{Young Deok\} and Kim, \{Hye Jung\} and Pil Kim",

year = "2005",

month = jun,

language = "English",

volume = "33",

pages = "106--111",

journal = "Microbiology and Biotechnology Letters",

issn = "1598-642X",

publisher = "Korean Society for Microbiolog and Biotechnology",

number = "2",

}

TY - JOUR

T1 - Substrate variety of a non-metal dependent tagatose-6-phosphate isomerase from Staphylococcus aureus

AU - Oh, Deok Kun

AU - Ji, Eun Soo

AU - Kwon, Young Deok

AU - Kim, Hye Jung

AU - Kim, Pil

PY - 2005/6

Y1 - 2005/6

N2 - To investigate the substrate variety of a putative non-metal dependent isomerase, the tagatose-6-phosphate isomerase (E.C. 5.3.1.26) structural genes (lacB; 510bp and lacA; 430bp) of Staphylococcus aureus were subcloned and co-expressed. Based on the substrate configuration, various aldoses were surveyed for substrate of ketose isomerization. Among the 10 aldoses tested, D-ribose and D-allose were isomerized by the enzyme. The subunit A and B showed more than 95% activity for D-ribose and 75% for D-allose in the presence of 1mM EDTA compared with non-EDTA conditions, which implying tagatose-6-phosphate isomerase is a non-metal dependent isomerase. Each of subunit A or subunit B alone showed no activity for any of the substrates tested. The affinity constant (Km) of tagatose-6-phosphate isomerase against D-ribose and D-allose were 26 mM and 142 mM, respectively.

AB - To investigate the substrate variety of a putative non-metal dependent isomerase, the tagatose-6-phosphate isomerase (E.C. 5.3.1.26) structural genes (lacB; 510bp and lacA; 430bp) of Staphylococcus aureus were subcloned and co-expressed. Based on the substrate configuration, various aldoses were surveyed for substrate of ketose isomerization. Among the 10 aldoses tested, D-ribose and D-allose were isomerized by the enzyme. The subunit A and B showed more than 95% activity for D-ribose and 75% for D-allose in the presence of 1mM EDTA compared with non-EDTA conditions, which implying tagatose-6-phosphate isomerase is a non-metal dependent isomerase. Each of subunit A or subunit B alone showed no activity for any of the substrates tested. The affinity constant (Km) of tagatose-6-phosphate isomerase against D-ribose and D-allose were 26 mM and 142 mM, respectively.

KW - Non-metal dependent isomerase

KW - Staphylococcus aureus

KW - Substrate variety

KW - Tagatose-6-phosphate isomerase

UR - https://www.scopus.com/pages/publications/22544437618

M3 - Article

AN - SCOPUS:22544437618

SN - 1598-642X

VL - 33

SP - 106

EP - 111

JO - Microbiology and Biotechnology Letters

JF - Microbiology and Biotechnology Letters

IS - 2

ER -

Substrate variety of a non-metal dependent tagatose-6-phosphate isomerase from Staphylococcus aureus

Abstract

Keywords

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