Mn<sup>2+</sup>in<scp>D</scp>-Glucosaminate Dehydratase from<i>Pseudomonas fluorescens</i>

Iwamoto, Ryoko; Nakura, Satomi

doi:10.1271/bbb.57.1058

Cited by 4 publications

(1 citation statement)

References 6 publications

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“…We have reported that GADH contains Mn 2 + ion near its active site and the Mn 2 + ion appears to stabilize the active site. 6 ) These results suggest that phosphate groups might chelate Mn 2 + ions that are involved in reaction (A) directly. Therefore, we measured the extent of inhibition caused by various derivatives of glycerol [analogues of the substrate or product of reaction (A)] in KPB and in VB (Table III).…”

Section: Effects Of Glycerol Derivatives On the Aldolase (A) And Dehymentioning

confidence: 82%

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion

Iwamoto¹,

Taniki²,

Koishi³

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Section: Effects Of Glycerol Derivatives On the Aldolase (A) And Dehymentioning

confidence: 82%

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion

Iwamoto¹,

Taniki²,

Koishi³

et al. 1995

Bioscience, Biotechnology, and Biochemistry

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Serine racemase homologue ofSaccharomyces cerevisiaehas l-threo-3-hydroxyaspartate dehydratase activity

Wada

Nakamori

Takagi

2003

FEMS Microbiology Letters

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The NH 2 -terminal amino acid sequence of L-threo-3-hydroxyaspartate dehydratase from Pseudomonas sp. T62 showed significant similarity to that of the SRY1 gene product of Saccharomyces cerevisiae (serine racemase in yeast). SRY1 was cloned and expressed in Escherichia coli, and the gene product was purified and partially characterized. The SRY1 gene product exhibited dehydratase activity specific for L-threo-3-hydroxyaspartate (K m = 3.9 mM, V max = 110 Wmol min 31 (mg protein) 31 ) but not for D-threo-or DL-erythro-3-hydroxyaspartate. The purified enzyme showed no detectable serine racemase activity. The activity of the enzyme was inhibited by hydroxylamine and EDTA, and was activated by Mg 2þ , Ca 2þ , and Mn 2þ , suggesting that pyridoxal-5P-phosphate and divalent cations participate in the enzyme reaction. Gene disruption and overexpression indicated that SRY1 is responsible for the 3-hydroxyaspartate resistance of S. cerevisiae. To our knowledge, this is the first report of 3-hydroxyaspartate dehydratase activity in eukaryotic cells.

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Purification and characterization of a novel enzyme, ?-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62

Wada¹

1999

FEMS Microbiology Letters

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L-threo-3-Hydroxyaspartate dehydratase (L-threo-3-hydroxyaspartate hydro-lyase), which exhibited specificity for L-threo-3hydroxyaspartate (K m = 0.74 mM, V max = 37.5 Wmol min 31 (mg protein) 31 ) but not for D-threo or D,L-erythro-3hydroxyaspartate, was purified from a cell-free extract of Pseudomonas sp. T62. The activity of the enzyme was inhibited by hydroxylamine and EDTA, which suggests that pyridoxal 5P-phosphate and divalent cations participate in the enzyme reaction. The NH 2 -terminal amino acid sequence showed significant similarity to the Saccharomyces cerevisiae YKL218c gene product, a hypothetical threonine dehydratase. However, the purified enzyme showed no threonine dehydratase activity. ß

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Mn²⁺inD-Glucosaminate Dehydratase fromPseudomonas fluorescens

Cited by 4 publications

References 6 publications

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion

Serine racemase homologue ofSaccharomyces cerevisiaehas l-threo-3-hydroxyaspartate dehydratase activity

Purification and characterization of a novel enzyme, ?-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62

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Mn2+inD-Glucosaminate Dehydratase fromPseudomonas fluorescens

Cited by 4 publications

References 6 publications

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn2+Ion

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn2+Ion

Serine racemase homologue ofSaccharomyces cerevisiaehas l-threo-3-hydroxyaspartate dehydratase activity

Purification and characterization of a novel enzyme, ?-threo-3-hydroxyaspartate dehydratase, from Pseudomonas sp. T62

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Mn²⁺inD-Glucosaminate Dehydratase fromPseudomonas fluorescens

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion

D-Glucosaminate Aldolase Activity ofD-Glucosaminate Dehydratase fromPseudomonas fluorescensand Its Requirement for Mn²⁺Ion