Characterization of a novel type homoserine dehydrogenase with high oxidation activity from Arthrobacter nicotinovorans

Liang, Xujun; Deng, Huaxiang; Bai, Yajun; Fan, Tai‐Ping; Zheng, Xiaohui; Cai, Yujie

doi:10.1016/j.procbio.2022.01.019

Cited by 3 publications

(3 citation statements)

References 61 publications

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“…Interestingly, Rlv UPM791 encodes two HSDs (RLV_0467 and RLV_4488) showing very distant relationship (26.9% identity). One of the proteins (RLV_0467) belongs to a novel family of HSDs recently described in Arthrobacter nicotinovorans and showing a strong unidirectionality toward oxidation of L-Hse into L-Asa ( Liang et al, 2022 ). These authors hypothesized that members of this novel group of HSDs evolved in homoserine-rich habitats to effectively use this compound as a source of carbon and/or nitrogen, a situation likely to occur in pea rhizosphere.…”

Section: Discussionmentioning

confidence: 99%

A host-specific diaminobutyrate aminotransferase contributes to symbiotic performance, homoserine metabolism, and competitiveness in the Rhizobium leguminosarum/Pisum sativum system

Ballesteros-Gutiérrez,

Albareda,

Barbas

et al. 2023

Front. Microbiol.

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Rhizobium leguminosarum bv. viciae (Rlv) UPM791 effectively nodulates pea and lentil, but bacteroids contain a number of proteins differentially expressed depending on the host. One of these host-dependent proteins (C189) is similar to a diaminobutyrate-2-oxoglutarate aminotransferase (DABA-AT). DABA-AT activity was demonstrated with cell extracts and with purified protein, so C189 was renamed as Dat. The dat gene was strongly induced in the central, active area of pea nodules, but not in lentil. Mutants defective in dat were impaired in symbiotic performance with pea plants, exhibiting reduced shoot dry weight, smaller nodules, and a lower competitiveness for nodulation. In contrast, there were no significant differences between mutant and wild-type in symbiosis with lentil plants. A comparative metabolomic approach using cell-free extracts from bacteroids induced in pea and lentil showed significant differences among the strains in pea bacteroids whereas no significant differences were found in lentil. Targeted metabolomic analysis revealed that the dat mutation abolished the presence of 2,4-diaminobutyrate (DABA) in pea nodules, indicating that DABA-AT reaction is oriented toward the production of DABA from L-aspartate semialdehyde. This analysis also showed the presence of L-homoserine, a likely source of aspartate semialdehyde, in pea bacteroids but not in those induced in lentil. The dat mutant showed impaired growth when cells were grown with L-homoserine as nitrogen source. Inclusion of DABA or L-homoserine as N source suppressed pantothenate auxotropy in Rlv UPM791, suggesting DABA as source of the pantothenate precursor β-alanine. These data indicate that Rlv UPM791 Dat enzyme is part of an adaptation mechanism of this bacterium to a homoserine-rich environment such as pea nodule and rhizosphere.

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Section: Discussionmentioning

confidence: 99%

A host-specific diaminobutyrate aminotransferase contributes to symbiotic performance, homoserine metabolism, and competitiveness in the Rhizobium leguminosarum/Pisum sativum system

Ballesteros-Gutiérrez,

Albareda,

Barbas

et al. 2023

Front. Microbiol.

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“…The canavanine degradation operon described here facilitates the oxidation of released homoserine to aspartate–semi-aldehyde by a member of a recently discovered new class of homoserine-dehydrogenases, 43 followed by oxidation to aspartate by either one of the two aldehyde-dehydrogenases (AC/AH) found induced by canavanine. Then, an ammonium-aspartate-lyase converts aspartate to fumarate and ammonia.…”

Section: Discussionmentioning

confidence: 99%

“…Comparing the sequence of HD to a recently discovered class of homoserine-dehydrogenases showed moderate sequence identity (59.6%). 43 Members of this new class favour the oxidation of homoserine rather than the reverse reaction taking place in the last step of the homoserine biosynthesis. The identified HD also displays the reported change in the NAD(P) + binding motif, explaining why HD rejects NADP + as co-substrate.…”

Section: Characterization Of Homoserine-dehydrogenase Aldehyde-dehydr...mentioning

confidence: 99%

Canavanine utilization via homoserine and hydroxyguanidine by a PLP-dependent γ-lyase in Pseudomonadaceae and Rhizobiales

et al. 2022

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Inoculation of wheat with Bacillus sp. wp-6 altered amino acid and flavonoid metabolism and promoted plant growth

et al. 2022

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Characterization of a novel type homoserine dehydrogenase with high oxidation activity from Arthrobacter nicotinovorans

Cited by 3 publications

References 61 publications

A host-specific diaminobutyrate aminotransferase contributes to symbiotic performance, homoserine metabolism, and competitiveness in the Rhizobium leguminosarum/Pisum sativum system

A host-specific diaminobutyrate aminotransferase contributes to symbiotic performance, homoserine metabolism, and competitiveness in the Rhizobium leguminosarum/Pisum sativum system

Canavanine utilization via homoserine and hydroxyguanidine by a PLP-dependent γ-lyase in Pseudomonadaceae and Rhizobiales

Inoculation of wheat with Bacillus sp. wp-6 altered amino acid and flavonoid metabolism and promoted plant growth

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