The yjjN of E. coli codes for an l-galactonate dehydrogenase and can be used for quantification of l-galactonate and l-gulonate

Joosu Kuivanen (Corresponding Author), Peter Richard

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)

Abstract

Escherichia coli is able to utilize l-galactonate as a sole carbon source. A metabolic pathway for l-galactonate catabolism is described in E. coli, and it is known to be interconnected with d-galacturonate metabolism. The corresponding gene encoding the first enzyme in the l-galactonate pathway, l-galactonate-5-dehydrogenase, was suggested to be yjjN. However, l-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an l-galactonate dehydrogenase having activity also for l-gulonate. The Km and kcat for l-galactonate were 19.5 ± 0.6 mM and 0.51 ± 0.03 s-1, respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for l-galactonate and l-gulonate were 1.65 and 10 µM, respectively.
Original languageEnglish
Pages (from-to)1829-1835
Number of pages7
JournalApplied Biochemistry and Biotechnology
Volume173
Issue number7
DOIs
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed

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Escherichia coli
Oxidoreductases
Gene encoding
Metabolic Networks and Pathways
Metabolism
Genes
Limit of Detection
Assays
Carbon
Enzymes
gulonic acid

Keywords

  • YjjN
  • l-galactonate-5-dehydrogenase
  • l-galactonate
  • l-gulonate
  • d-galacturonate
  • E.coli

Cite this

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title = "The yjjN of E. coli codes for an l-galactonate dehydrogenase and can be used for quantification of l-galactonate and l-gulonate",
abstract = "Escherichia coli is able to utilize l-galactonate as a sole carbon source. A metabolic pathway for l-galactonate catabolism is described in E. coli, and it is known to be interconnected with d-galacturonate metabolism. The corresponding gene encoding the first enzyme in the l-galactonate pathway, l-galactonate-5-dehydrogenase, was suggested to be yjjN. However, l-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an l-galactonate dehydrogenase having activity also for l-gulonate. The Km and kcat for l-galactonate were 19.5 ± 0.6 mM and 0.51 ± 0.03 s-1, respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for l-galactonate and l-gulonate were 1.65 and 10 µM, respectively.",
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language = "English",
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The yjjN of E. coli codes for an l-galactonate dehydrogenase and can be used for quantification of l-galactonate and l-gulonate. / Kuivanen, Joosu (Corresponding Author); Richard, Peter.

In: Applied Biochemistry and Biotechnology, Vol. 173, No. 7, 2014, p. 1829-1835.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - The yjjN of E. coli codes for an l-galactonate dehydrogenase and can be used for quantification of l-galactonate and l-gulonate

AU - Kuivanen, Joosu

AU - Richard, Peter

PY - 2014

Y1 - 2014

N2 - Escherichia coli is able to utilize l-galactonate as a sole carbon source. A metabolic pathway for l-galactonate catabolism is described in E. coli, and it is known to be interconnected with d-galacturonate metabolism. The corresponding gene encoding the first enzyme in the l-galactonate pathway, l-galactonate-5-dehydrogenase, was suggested to be yjjN. However, l-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an l-galactonate dehydrogenase having activity also for l-gulonate. The Km and kcat for l-galactonate were 19.5 ± 0.6 mM and 0.51 ± 0.03 s-1, respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for l-galactonate and l-gulonate were 1.65 and 10 µM, respectively.

AB - Escherichia coli is able to utilize l-galactonate as a sole carbon source. A metabolic pathway for l-galactonate catabolism is described in E. coli, and it is known to be interconnected with d-galacturonate metabolism. The corresponding gene encoding the first enzyme in the l-galactonate pathway, l-galactonate-5-dehydrogenase, was suggested to be yjjN. However, l-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an l-galactonate dehydrogenase having activity also for l-gulonate. The Km and kcat for l-galactonate were 19.5 ± 0.6 mM and 0.51 ± 0.03 s-1, respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for l-galactonate and l-gulonate were 1.65 and 10 µM, respectively.

KW - YjjN

KW - l-galactonate-5-dehydrogenase

KW - l-galactonate

KW - l-gulonate

KW - d-galacturonate

KW - E.coli

U2 - 10.1007/s12010-014-0969-0

DO - 10.1007/s12010-014-0969-0

M3 - Article

VL - 173

SP - 1829

EP - 1835

JO - Applied Biochemistry and Biotechnology

JF - Applied Biochemistry and Biotechnology

SN - 0273-2289

IS - 7

ER -