An enzymatic method to estimate the content of L-hydroxyproline

Watanabe, Shizuo; Hiraoka, Yoshinobu; Endo, Shiori; Tanimoto, Yoshiaki; Tozawa, Yuzuru; Watanabe, Yasuo

doi:10.1016/j.jbiotec.2015.01.026

Cited by 24 publications

(31 citation statements)

References 19 publications

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“…7A. The K m value of MvHypA2 was more than 10-fold lower than values of the HypG proteins (Cys/Thr) (16,20). Bifunctional T3LHyp dehydratase/2-epimerase.…”

Section: Resultsmentioning

confidence: 89%

“…As described in the Introduction, among metabolic enzymes involved in L-Hyp pathways, there are several examples of convergent evolution: for C4DHyp dehydrogenase, HypB and HypBCD (15,16); for C3LHyp dehydratase, HypI (AcnX Type I ) and HypG (24,28); for Pyr2C reductase, HypK and HypH (21). Furthermore, T3LHyp dehydratase appeared twice in the same proline racemase-superfamily: HypG and HypL (Fig.…”

Section: R Ni Tvf Ad Gevdr Spc Gs Gt Sar Ia L R Nv Vif Ad Gevdr Spc Gmentioning

confidence: 90%

“…The catabolism of L-Hyp, including T4LHyp, T3LHyp, and C3LHyp, by (micro)organisms has recently been investigated at the molecular level ( Fig. 2A to C and Table 1; see also Table S1 in the supplemental material) (12)(13)(14)(15)(16)(17)(18)(19)(20)(21).…”

mentioning

confidence: 99%

“…C4DHyp is then oxidized to Δ 1 -pyrroline-4R-hydroxy-2-carboxylate (HPC) by a flavincontaining C4DHyp dehydrogenase. Interestingly, there are two types of C4DHyp dehydrogenases: heteromeric-type enzymes encoded by the hypB, hypC, and hypD genes and homomeric-type enzymes encoded by the hypB gene (15,16). Both of the hypB genes are sequentially homologous with each other, and the HypB protein encoding the heteromeric-type enzyme exhibits full dehydrogenase activity by itself (the so-called catalytic subunit).…”

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confidence: 99%

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

et al. 2017

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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

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“…7A. The K m value of MvHypA2 was more than 10-fold lower than values of the HypG proteins (Cys/Thr) (16,20). Bifunctional T3LHyp dehydratase/2-epimerase.…”

Section: Resultsmentioning

confidence: 89%

Section: R Ni Tvf Ad Gevdr Spc Gs Gt Sar Ia L R Nv Vif Ad Gevdr Spc Gmentioning

confidence: 90%

mentioning

confidence: 99%

mentioning

confidence: 99%

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

et al. 2017

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“…Additionally, the latter D-hydroxyproline dehydrogenase, in contrast to the former, can be stored for a few months at least, suggesting the possibility that it could have bioindustrial applications. Although an efficient system for preparation of the recombinant enzyme has not been reported, in a recent study we successfully functionally expressed heteromeric D-hydroxyproline dehydrogenase from Azospirillum brasilense instead of P. aeruginosa in Escherichia coli cells [22].…”

Section: Introductionmentioning

confidence: 99%

A bienzyme electrochemical biosensor for the detection of collagen l-hydroxyproline

Sakamoto

Watanabe

Koto

et al. 2015

Sensing and Bio-Sensing Research

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L-hydroxyproline L-hydroxyproline epimerase D-hydroxyproline dehydrogenase a b s t r a c t L-hydroxyproline (L-Hyp: trans-4-hydroxy-L-proline) is commonly found at high concentrations in connective tissue proteins such as collagen. It is a remarkably useful molecular marker because variation in the level of L-Hyp is associated with various diseases. Recently, the novel enzymes L-hydroxyproline epimerase and D-hydroxyproline dehydrogenase were isolated from bacteria. In this study, a novel electrochemical biosensor for L-Hyp was constructed using these two enzymes. L-hydroxyproline epimerase epimerized L-Hyp to D-hydroxyproline (D-Hyp: cis-4-hydroxy-D-proline), and D-Hyp was oxidized with the reaction catalyzed by D-hydroxyproline dehydrogenase and mediated by ferrocene. We found that the sensor could determine L-Hyp concentrations of 10-100 lM with high-selectivity.

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Comparative study of collagen distribution in the dermis of the embryonic carapace of soft‐ and hard‐shelled cryptodiran turtles

Yang

Song

et al. 2021

Journal of Morphology

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Turtles are characterized by their typical carapace, which is primarily composed of corneous beta proteins in the horny part and collagen in the dermal part. The formation of the extracellular matrix in the dermis of the carapace in a hard‐shelled and a soft‐shelled turtle has been compared. The study examines carapace development, with an emphasis on collagen accumulation, in the soft‐shelled turtle Pelodiscus sinensis and hard‐shelled turtle Trachemys scripta elegans, using comparative morphological and embryological analyses. The histological results showed that collagen deposition in the turtle carapace increased as the embryos developed. However, significant differences were observed between the two turtle species at the developmental stages examined. The microstructure of the dermis of the carapace of P. sinensis showed light and dark banding of collagen bundles, with a higher overall collagen content, whereas the carapacial matrix of T. scripta was characterized by loosely packed and thinner collagenous fiber bundles with a lower percentage of type I collagen. Overall, the formation and distribution of collagen fibrils at specific developmental stages are different between the soft‐and hard‐shelled turtles. These results indicate that the pliable epidermis of the soft‐shelled turtle is supported by a strong dermis that is regularly distributed with collagen and that it allows improved maneuvering, whereas a strong but inflexible epidermis as observed in case of hard‐shelled turtles limits movement.

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An enzymatic method to estimate the content of L-hydroxyproline

Cited by 24 publications

References 19 publications

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

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

A bienzyme electrochemical biosensor for the detection of collagen l-hydroxyproline

Comparative study of collagen distribution in the dermis of the embryonic carapace of soft‐ and hard‐shelled cryptodiran turtles

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