Identification and Characterization of Bifunctional Proline Racemase/Hydroxyproline Epimerase from Archaea: Discrimination of Substrates and Molecular Evolution

Watanabe, Shizuo; Tanimoto, Yoshiaki; Nishiwaki, Hisashi; Watanabe, Yasuo

doi:10.1371/journal.pone.0120349

Cited by 14 publications

(11 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1B. Together with other reports (12,25,59,(62)(63)(64), this report defines the genes that encode specific enzyme activities required for trans-4-hydroxy-L-proline catabolism. These studies should allow the identification of hydroxyproline catabolic genes in other organisms where many of these genes are annotated as genes of unknown function.…”

Section: Discussionmentioning

confidence: 56%

See 1 more Smart Citation

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

et al. 2016

View full text Add to dashboard Cite

Sinorhizobium meliloti IMPORTANCEHydroxyproline is abundant in proteins in animal and plant tissues and serves as a carbon and a nitrogen source for bacteria in diverse environments, including the rhizosphere, compost, and the mammalian gut. While the main biochemical features of bacterial hydroxyproline catabolism were elucidated in the 1960s, the genetic and molecular details have only recently been determined. Elucidating the genetics of hydroxyproline catabolism will aid in the annotation of these genes in other genomes and metagenomic libraries. This will facilitate an improved understanding of the importance of this pathway and may assist in determining the prevalence of hydroxyproline in a particular environment.4-Hydroxyproline and 3-hydroxyproline in animal and plant proteins are formed through the posttranslational modification of proline residues by the enzyme proline hydroxylase. In some bacteria, hydroxyproline is synthesized from free L-proline, where it is employed in the synthesis of secondary metabolites (1, 2). 4-Hydroxyproline has two chiral carbon atoms, and of its four isomeric forms, trans-4-hydroxy-L-proline (trans-4-L-Hyp) and cis-4-hydroxy-D-proline (cis-4-D-Hyp) appear to be the two most common isomers. trans-4-

show abstract

Section: Discussionmentioning

confidence: 56%

“…The partial-growth as opposed to the no-growth phenotype of the hypH and hypO mutants can be attributed to the presence of alternate enzyme activities. HypO is (20,49,64,65,67). Abbreviations: Pyr5C, ⌬ 1 -pyrroline-5-carboxylate; Pyr2C, ⌬ 1 -pyrroline-2-carboxylate; ␥-glutamyl-5-P, ␥-glutamyl-5-phosphate; Pi, phosphate.…”

Section: Discussionmentioning

confidence: 99%

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

et al. 2016

View full text Add to dashboard Cite

show abstract

“…In order to correctly analyze 2-epimerase activity, we enzymatically synthesized C3DHyp (unavailable commercially) from T3LHyp (12). Specific activity values for the disappearance of C3DHyp (2.08) and production of T3LHyp (2.27) were similar to the value obtained for the production of C3DHyp from T3LHyp (Fig.…”

Section: V M Ph Ak Gs S S S S Sv L L a M Rs Gr Gs S S S S Yv L L A mentioning

confidence: 56%

“…2D), indicating that this gene cluster is related to the metabolism of not only T4LHyp but also C3LHyp and/or T3LHyp. Hydroxyproline 2-epimerase (Cys/Cys) and T3LHyp dehydratase (Cys/Thr, Ser/Cys, or Ser/Thr) are considered to belong to the same proline racemase superfamily, together with the archetype proline racemase (Cys/Cys), and have been classified into four types based on two specific residues at the active sites (shown in parentheses) (12,(19)(20)(21). Both the MvHypA1 (GA0074695_2673) and MvHypA2 (GA0074695_2680) proteins containing the L-Hyp gene cluster possessed two cysteine residues at their active sites (Cys 91 /Cys 254 and Cys 90 /Cys 256 , respectively) specific for hydroxyproline 2-epimerase (and proline racemase) but not T3LHyp dehydratase (Fig.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of a Novel cis -3-Hydroxy- l -Proline Dehydratase and a trans -3-Hydroxy- l -Proline Dehydratase from Bacteria

et al. 2017

Self Cite

View full text Add to dashboard Cite

Hydroxyprolines, such as trans-4-hydroxy-L-proline (T4LHyp), trans-3-hydroxy-L-proline (T3LHyp), and cis-3-hydroxy-L-proline (C3LHyp), are present in some proteins including collagen, plant cell wall, and several peptide antibiotics. In bacteria, genes involved in the degradation of hydroxyproline are often clustered on the genome (L-Hyp gene cluster). We recently reported that an aconitase X (AcnX)-like hypI gene from an L-Hyp gene cluster functions as a monomeric C3LHyp dehydratase (AcnX Type I ). However, the physiological role of C3LHyp dehydratase remained unclear. We here demonstrate that Azospirillum brasilense NBRC 102289, an aerobic nitrogen-fixing bacterium, robustly grows using not only T4LHyp and T3LHyp but also C3LHyp as the sole carbon source. The small and large subunits of the hypI gene (hypI S and hypI L , respectively) from A. brasilense NBRC 102289 are located separately from the L-Hyp gene cluster and encode a C3LHyp dehydratase with a novel heterodimeric structure (AcnX Type IIa ). A strain disrupted in the hypI S gene did not grow on C3LHyp, suggesting its involvement in C3LHyp metabolism. Furthermore, C3LHyp induced transcription of not only the hypI genes but also the hypK gene encoding Δ 1 -pyrroline-2-carboxylate reductase, which is involved in T3LHyp, D-proline, and D-lysine metabolism. On the other hand, the L-Hyp gene cluster of some other bacteria contained not only the AcnX Type IIa gene but also two putative proline racemase-like genes (hypA1 and hypA2). Despite having the same active sites (a pair of Cys/Cys) as hydroxyproline 2-epimerase, which is involved in the metabolism of T4LHyp, the dominant reaction by HypA2 was clearly the dehydration of T3LHyp, a novel type of T3LHyp dehydratase that differed from the known enzyme (Cys/Thr). L-hydroxyproline) degradation in aerobic bacteria, its genetic and molecular information has only recently been elucidated. L-Hydroxyproline metabolic genes are often clustered on bacterial genomes. These loci frequently contain a hypothetical gene(s), whose novel enzyme functions are related to the metabolism of trans-3-hydroxyL-proline and/or cis-3-hydroxyL-proline, a relatively rare L-hydroxyproline in nature. Several L-hydroxyproline metabolic enzymes show no sequential similarities, suggesting their emergence by convergent evolution. Furthermore, transcriptional regulation by trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and/or cis-3-hydroxy-L-proline significantly differs between bacteria. The results of the present study show that several L-hydroxyprolines are available for bacteria as carbon and energy sources and may contribute to the discovery of potential metabolic pathways of another hydroxyproline(s). IMPORTANCE More than 50 years after the discovery of trans-4-hydroxy-L-proline (generally calledKEYWORDS aconitase X, proline racemase superfamily, gene cluster, hydroxyproline, convergent evolution

show abstract

Enzymatic reactions and microorganisms producing the various isomers of hydroxyproline

Kino

2020

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Identification and Characterization of Bifunctional Proline Racemase/Hydroxyproline Epimerase from Archaea: Discrimination of Substrates and Molecular Evolution

Cited by 14 publications

References 33 publications

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

l-Hydroxyproline andd-Proline Catabolism in Sinorhizobium meliloti

Characterization of a Novel cis -3-Hydroxy- l -Proline Dehydratase and a trans -3-Hydroxy- l -Proline Dehydratase from Bacteria

Enzymatic reactions and microorganisms producing the various isomers of hydroxyproline

Contact Info

Product

Resources

About