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Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis.

Plants (Basel, Switzerland)

Sánchez-Parra B, Frerigmann H, Alonso MM, Loba VC, Jost R, Hentrich M, Pollmann S.
PMID: 27135507
Plants (Basel). 2014 Aug 07;3(3):324-47. doi: 10.3390/plants3030324.

Amidases [EC 3.5.1.4] capable of converting indole-3-acetamide (IAM) into the major plant growth hormone indole-3-acetic acid (IAA) are assumed to be involved in auxin de novo biosynthesis. With the emerging amount of genomics data, it was possible to identify...

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Sánchez-Parra B, Frerigmann H, Alonso MM, et al. Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. Plants (Basel). 2014;3(3):324-47doi: 10.3390/plants3030324.
Sánchez-Parra, B., Frerigmann, H., Alonso, M. M., Loba, V. C., Jost, R., Hentrich, M., & Pollmann, S. (2014). Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. Plants (Basel, Switzerland), 3(3), 324-47. https://doi.org/10.3390/plants3030324
Sánchez-Parra, Beatriz, et al. "Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis." Plants (Basel, Switzerland) vol. 3,3 (2014): 324-47. doi: https://doi.org/10.3390/plants3030324
Sánchez-Parra B, Frerigmann H, Alonso MM, Loba VC, Jost R, Hentrich M, Pollmann S. Characterization of Four Bifunctional Plant IAM/PAM-Amidohydrolases Capable of Contributing to Auxin Biosynthesis. Plants (Basel). 2014 Aug 07;3(3):324-47. doi: 10.3390/plants3030324. PMID: 27135507; PMCID: PMC4844348.
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pncA Mutations in the Specimens from Extrapulmonary Tuberculosis.

Tuberculosis and respiratory diseases

Lee J, Yun YJ, Kqueen CY, Lee JH, Kim HY, Kim YR, Kook YH, Lee KH.
PMID: 23101013
Tuberc Respir Dis (Seoul). 2012 Jun;72(6):475-80. doi: 10.4046/trd.2012.72.6.475. Epub 2012 Jun 29.

BACKGROUND: Pyrazinamide (PZA) is an effective antitubercular drug that becomes toxic to Mycobacterium tuberculosis when converted to pyrazinoic acid by pyrazinamidase (PZase), encoded by mycobacterial pncA. A strong association was noted between the loss of PZase activity and PZA...

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Lee J, Yun YJ, Kqueen CY, et al. pncA Mutations in the Specimens from Extrapulmonary Tuberculosis. Tuberc Respir Dis (Seoul). 2012;72(6):475-80doi: 10.4046/trd.2012.72.6.475.
Lee, J., Yun, Y. J., Kqueen, C. Y., Lee, J. H., Kim, H. Y., Kim, Y. R., Kook, Y. H., & Lee, K. H. (2012). pncA Mutations in the Specimens from Extrapulmonary Tuberculosis. Tuberculosis and respiratory diseases, 72(6), 475-80. https://doi.org/10.4046/trd.2012.72.6.475
Lee, Jaechun, et al. "pncA Mutations in the Specimens from Extrapulmonary Tuberculosis." Tuberculosis and respiratory diseases vol. 72,6 (2012): 475-80. doi: https://doi.org/10.4046/trd.2012.72.6.475
Lee J, Yun YJ, Kqueen CY, Lee JH, Kim HY, Kim YR, Kook YH, Lee KH. pncA Mutations in the Specimens from Extrapulmonary Tuberculosis. Tuberc Respir Dis (Seoul). 2012 Jun;72(6):475-80. doi: 10.4046/trd.2012.72.6.475. Epub 2012 Jun 29. PMID: 23101013; PMCID: PMC3475457.
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Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress.

Rice (New York, N.Y.)

Hazman M, Sühnel M, Schäfer S, Zumsteg J, Lesot A, Beltran F, Marquis V, Herrgott L, Miesch L, Riemann M, Heitz T.
PMID: 31240493
Rice (N Y). 2019 Jun 25;12(1):45. doi: 10.1186/s12284-019-0303-0.

BACKGROUND: Jasmonate (JA) signaling and functions have been established in rice development and response to a range of biotic or abiotic stress conditions. However, information on the molecular actors and mechanisms underlying turnover of the bioactive jasmonoyl-isoleucine (JA-Ile) is...

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Hazman M, Sühnel M, Schäfer S, et al. Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress. Rice (N Y). 2019;12(1):45doi: 10.1186/s12284-019-0303-0.
Hazman, M., Sühnel, M., Schäfer, S., Zumsteg, J., Lesot, A., Beltran, F., Marquis, V., Herrgott, L., Miesch, L., Riemann, M., & Heitz, T. (2019). Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress. Rice (New York, N.Y.), 12(1), 45. https://doi.org/10.1186/s12284-019-0303-0
Hazman, Mohamed, et al. "Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress." Rice (New York, N.Y.) vol. 12,1 (2019): 45. doi: https://doi.org/10.1186/s12284-019-0303-0
Hazman M, Sühnel M, Schäfer S, Zumsteg J, Lesot A, Beltran F, Marquis V, Herrgott L, Miesch L, Riemann M, Heitz T. Characterization of Jasmonoyl-Isoleucine (JA-Ile) Hormonal Catabolic Pathways in Rice upon Wounding and Salt Stress. Rice (N Y). 2019 Jun 25;12(1):45. doi: 10.1186/s12284-019-0303-0. PMID: 31240493; PMCID: PMC6592992.
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Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms.

Recent patents on biotechnology

de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF.
PMID: 34353277
Recent Pat Biotechnol. 2021 Aug 05; doi: 10.2174/1872208315666210805162459. Epub 2021 Aug 05.

BACKGROUND: L-asparaginase (L-ASNase, L-asparagine amidohydrolase, E.C.3.5.1.1) is an enzyme with wide therapeutic applicability. Currently, the commercialized L-ASNase comes from mesophilic organisms, presenting low specificity to the substrate and limitations regarding thermostability and active pH range. Such factors prevent the...

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de Oliveira Lima IG, Bispo JRS, da Silva MB, et al. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021;doi: 10.2174/1872208315666210805162459.
de Oliveira Lima, I. G., Bispo, J. R. S., da Silva, M. B., de Oliveira Feitosa, A., Dos Santos, A. C. M., Moreira, M. S. A., Passarini, M. R. Z., Saraiva Câmara, P. E. A., Rosa, L. H., Oliveira, V. M., de Queiroz, A. C., & Duarte, A. W. F. (2021). Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent patents on biotechnology, . https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima, Igor Gomes, et al. "Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms." Recent patents on biotechnology vol. (2021). doi: https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021 Aug 05; doi: 10.2174/1872208315666210805162459. Epub 2021 Aug 05. PMID: 34353277.
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The main oxidative inactivation pathway of the plant hormone auxin.

Nature communications

Hayashi KI, Arai K, Aoi Y, Tanaka Y, Hira H, Guo R, Hu Y, Ge C, Zhao Y, Kasahara H, Fukui K.
PMID: 34811366
Nat Commun. 2021 Nov 22;12(1):6752. doi: 10.1038/s41467-021-27020-1.

Inactivation of the phytohormone auxin plays important roles in plant development, and several enzymes have been implicated in auxin inactivation. In this study, we show that the predominant natural auxin, indole-3-acetic acid (IAA), is mainly inactivated via the GH3-ILR1-DAO...

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Hayashi KI, Arai K, Aoi Y, et al. The main oxidative inactivation pathway of the plant hormone auxin. Nat Commun. 2021;12(1):6752doi: 10.1038/s41467-021-27020-1.
Hayashi, K. I., Arai, K., Aoi, Y., Tanaka, Y., Hira, H., Guo, R., Hu, Y., Ge, C., Zhao, Y., Kasahara, H., & Fukui, K. (2021). The main oxidative inactivation pathway of the plant hormone auxin. Nature communications, 12(1), 6752. https://doi.org/10.1038/s41467-021-27020-1
Hayashi, Ken-Ichiro, et al. "The main oxidative inactivation pathway of the plant hormone auxin." Nature communications vol. 12,1 (2021): 6752. doi: https://doi.org/10.1038/s41467-021-27020-1
Hayashi KI, Arai K, Aoi Y, Tanaka Y, Hira H, Guo R, Hu Y, Ge C, Zhao Y, Kasahara H, Fukui K. The main oxidative inactivation pathway of the plant hormone auxin. Nat Commun. 2021 Nov 22;12(1):6752. doi: 10.1038/s41467-021-27020-1. PMID: 34811366.
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The main oxidative inactivation pathway of the plant hormone auxin.

Nature communications

Hayashi KI, Arai K, Aoi Y, Tanaka Y, Hira H, Guo R, Hu Y, Ge C, Zhao Y, Kasahara H, Fukui K.
PMID: 34811366
Nat Commun. 2021 Nov 22;12(1):6752. doi: 10.1038/s41467-021-27020-1.

Inactivation of the phytohormone auxin plays important roles in plant development, and several enzymes have been implicated in auxin inactivation. In this study, we show that the predominant natural auxin, indole-3-acetic acid (IAA), is mainly inactivated via the GH3-ILR1-DAO...

Cite
Hayashi KI, Arai K, Aoi Y, et al. The main oxidative inactivation pathway of the plant hormone auxin. Nat Commun. 2021;12(1):6752doi: 10.1038/s41467-021-27020-1.
Hayashi, K. I., Arai, K., Aoi, Y., Tanaka, Y., Hira, H., Guo, R., Hu, Y., Ge, C., Zhao, Y., Kasahara, H., & Fukui, K. (2021). The main oxidative inactivation pathway of the plant hormone auxin. Nature communications, 12(1), 6752. https://doi.org/10.1038/s41467-021-27020-1
Hayashi, Ken-Ichiro, et al. "The main oxidative inactivation pathway of the plant hormone auxin." Nature communications vol. 12,1 (2021): 6752. doi: https://doi.org/10.1038/s41467-021-27020-1
Hayashi KI, Arai K, Aoi Y, Tanaka Y, Hira H, Guo R, Hu Y, Ge C, Zhao Y, Kasahara H, Fukui K. The main oxidative inactivation pathway of the plant hormone auxin. Nat Commun. 2021 Nov 22;12(1):6752. doi: 10.1038/s41467-021-27020-1. PMID: 34811366; PMCID: PMC8608799.
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Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms.

Recent patents on biotechnology

de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF.
PMID: 34353277
Recent Pat Biotechnol. 2021;15(4):250-265. doi: 10.2174/1872208315666210805162459.

BACKGROUND: L-asparaginase (L-ASNase, L-asparagine amidohydrolase, E.C.3.5.1.1) is an enzyme with wide therapeutic applicability. Currently, the commercialized L-ASNase comes from mesophilic organisms, presenting low specificity to the substrate and limitations regarding thermostability and active pH range. Such factors prevent the...

Cite
de Oliveira Lima IG, Bispo JRS, da Silva MB, et al. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021;15(4):250-265doi: 10.2174/1872208315666210805162459.
de Oliveira Lima, I. G., Bispo, J. R. S., da Silva, M. B., de Oliveira Feitosa, A., Dos Santos, A. C. M., Moreira, M. S. A., Passarini, M. R. Z., Saraiva Câmara, P. E. A., Rosa, L. H., Oliveira, V. M., de Queiroz, A. C., & Duarte, A. W. F. (2021). Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent patents on biotechnology, 15(4), 250-265. https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima, Igor Gomes, et al. "Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms." Recent patents on biotechnology vol. 15,4 (2021): 250-265. doi: https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021;15(4):250-265. doi: 10.2174/1872208315666210805162459. PMID: 34353277.
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Structural Analysis of .

Molecules (Basel, Switzerland)

Guan HH, Huang YH, Lin ES, Chen CJ, Huang CY.
PMID: 34885830
Molecules. 2021 Nov 29;26(23). doi: 10.3390/molecules26237249.

Dihydroorotase (DHOase), a dimetalloenzyme containing a carbamylated lysine within the active site, is a member of the cyclic amidohydrolase family, which also includes allantoinase (ALLase), dihydropyrimidinase (DHPase), hydantoinase, and imidase. Unlike most known cyclic amidohydrolases, which are tetrameric, DHOase...

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Guan HH, Huang YH, Lin ES, et al. Structural Analysis of . Molecules. 2021;26(23)doi: 10.3390/molecules26237249.
Guan, H. H., Huang, Y. H., Lin, E. S., Chen, C. J., & Huang, C. Y. (2021). Structural Analysis of . Molecules (Basel, Switzerland), 26(23), . https://doi.org/10.3390/molecules26237249
Guan, Hong-Hsiang, et al. "Structural Analysis of ." Molecules (Basel, Switzerland) vol. 26,23 (2021). doi: https://doi.org/10.3390/molecules26237249
Guan HH, Huang YH, Lin ES, Chen CJ, Huang CY. Structural Analysis of . Molecules. 2021 Nov 29;26(23). doi: 10.3390/molecules26237249. PMID: 34885830.
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Structural Analysis of .

Molecules (Basel, Switzerland)

Guan HH, Huang YH, Lin ES, Chen CJ, Huang CY.
PMID: 34885830
Molecules. 2021 Nov 29;26(23). doi: 10.3390/molecules26237249.

Dihydroorotase (DHOase), a dimetalloenzyme containing a carbamylated lysine within the active site, is a member of the cyclic amidohydrolase family, which also includes allantoinase (ALLase), dihydropyrimidinase (DHPase), hydantoinase, and imidase. Unlike most known cyclic amidohydrolases, which are tetrameric, DHOase...

Cite
Guan HH, Huang YH, Lin ES, et al. Structural Analysis of . Molecules. 2021;26(23)doi: 10.3390/molecules26237249.
Guan, H. H., Huang, Y. H., Lin, E. S., Chen, C. J., & Huang, C. Y. (2021). Structural Analysis of . Molecules (Basel, Switzerland), 26(23), . https://doi.org/10.3390/molecules26237249
Guan, Hong-Hsiang, et al. "Structural Analysis of ." Molecules (Basel, Switzerland) vol. 26,23 (2021). doi: https://doi.org/10.3390/molecules26237249
Guan HH, Huang YH, Lin ES, Chen CJ, Huang CY. Structural Analysis of . Molecules. 2021 Nov 29;26(23). doi: 10.3390/molecules26237249. PMID: 34885830; PMCID: PMC8659124.
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Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries.

Frontiers in microbiology

Zapata-Pérez R, García-Saura AG, Jebbar M, Golyshin PN, Sánchez-Ferrer Á.
PMID: 28018295
Front Microbiol. 2016 Nov 29;7:1915. doi: 10.3389/fmicb.2016.01915. eCollection 2016.

Nicotinamidases catalyze the hydrolysis of the amide bond in nicotinamide (NAM) to produce ammonia and nicotinic acid (NA). These enzymes are an essential component of the NAD

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Zapata-Pérez R, García-Saura AG, Jebbar M, et al. Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries. Front Microbiol. 2016;7:1915doi: 10.3389/fmicb.2016.01915.
Zapata-Pérez, R., García-Saura, A. G., Jebbar, M., Golyshin, P. N., & Sánchez-Ferrer, �. �. (2016). Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries. Frontiers in microbiology, 71915. https://doi.org/10.3389/fmicb.2016.01915
Zapata-Pérez, Rubén, et al. "Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries." Frontiers in microbiology vol. 7 (2016): 1915. doi: https://doi.org/10.3389/fmicb.2016.01915
Zapata-Pérez R, García-Saura AG, Jebbar M, Golyshin PN, Sánchez-Ferrer Á. Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries. Front Microbiol. 2016 Nov 29;7:1915. doi: 10.3389/fmicb.2016.01915. eCollection 2016. PMID: 28018295; PMCID: PMC5147024.
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Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms.

Recent patents on biotechnology

de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF.
PMID: 34353277
Recent Pat Biotechnol. 2021;15(4):250-265. doi: 10.2174/1872208315666210805162459.

BACKGROUND: L-asparaginase (L-ASNase, L-asparagine amidohydrolase, E.C.3.5.1.1) is an enzyme with wide therapeutic applicability. Currently, the commercialized L-ASNase comes from mesophilic organisms, presenting low specificity to the substrate and limitations regarding thermostability and active pH range. Such factors prevent the...

Cite
de Oliveira Lima IG, Bispo JRS, da Silva MB, et al. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021;15(4):250-265doi: 10.2174/1872208315666210805162459.
de Oliveira Lima, I. G., Bispo, J. R. S., da Silva, M. B., de Oliveira Feitosa, A., Dos Santos, A. C. M., Moreira, M. S. A., Passarini, M. R. Z., Saraiva Câmara, P. E. A., Rosa, L. H., Oliveira, V. M., de Queiroz, A. C., & Duarte, A. W. F. (2021). Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent patents on biotechnology, 15(4), 250-265. https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima, Igor Gomes, et al. "Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms." Recent patents on biotechnology vol. 15,4 (2021): 250-265. doi: https://doi.org/10.2174/1872208315666210805162459
de Oliveira Lima IG, Bispo JRS, da Silva MB, de Oliveira Feitosa A, Dos Santos ACM, Moreira MSA, Passarini MRZ, Saraiva Câmara PEA, Rosa LH, Oliveira VM, de Queiroz AC, Duarte AWF. Technological Prospecting: Mapping Patents on L-asparaginases from Extremophilic Microorganisms. Recent Pat Biotechnol. 2021;15(4):250-265. doi: 10.2174/1872208315666210805162459. PMID: 34353277.
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Characterization of the metallo-dependent amidohydrolases responsible for "auxiliary" leucinyl removal in the biosynthesis of 2,2'-bipyridine antibiotics.

Synthetic and systems biotechnology

Chen M, Pang B, Du YN, Zhang YP, Liu W.
PMID: 29062971
Synth Syst Biotechnol. 2017 Jul 13;2(2):137-146. doi: 10.1016/j.synbio.2017.07.002. eCollection 2017 Jun.

2,2'-Bipyridine (2,2'-BiPy) is an attractive core structure present in a number of biologically active natural products, including the structurally related antibiotics caerulomycins (CAEs) and collismycins (COLs). Their biosynthetic pathways share a similar key 2,2'-BiPy-l-leucine intermediate, which is desulfurated or...

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Chen M, Pang B, Du YN, et al. Characterization of the metallo-dependent amidohydrolases responsible for "auxiliary" leucinyl removal in the biosynthesis of 2,2'-bipyridine antibiotics. Synth Syst Biotechnol. 2017;2(2):137-146doi: 10.1016/j.synbio.2017.07.002.
Chen, M., Pang, B., Du, Y. N., Zhang, Y. P., & Liu, W. (2017). Characterization of the metallo-dependent amidohydrolases responsible for "auxiliary" leucinyl removal in the biosynthesis of 2,2'-bipyridine antibiotics. Synthetic and systems biotechnology, 2(2), 137-146. https://doi.org/10.1016/j.synbio.2017.07.002
Chen, Ming, et al. "Characterization of the metallo-dependent amidohydrolases responsible for "auxiliary" leucinyl removal in the biosynthesis of 2,2'-bipyridine antibiotics." Synthetic and systems biotechnology vol. 2,2 (2017): 137-146. doi: https://doi.org/10.1016/j.synbio.2017.07.002
Chen M, Pang B, Du YN, Zhang YP, Liu W. Characterization of the metallo-dependent amidohydrolases responsible for "auxiliary" leucinyl removal in the biosynthesis of 2,2'-bipyridine antibiotics. Synth Syst Biotechnol. 2017 Jul 13;2(2):137-146. doi: 10.1016/j.synbio.2017.07.002. eCollection 2017 Jun. PMID: 29062971; PMCID: PMC5636949.
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Showing 1 to 12 of 20 entries