Halohydrin dehalogenase (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Halohydrin dehalogenase" in English language version.

refsWebsite

Global rank English rank

12nih.gov

4^th place

10doi.org

2^nd place

3semanticscholar.org

11^th place

8^th place

1rug.nl

2,779^th place

1,997^th place

1harvard.edu

18^th place

17^th place

doi.org

Fauzi AM, Hardman DJ, Bull AT (1996). "Biodehalogenation of low concentrations of 1,3-dichloropropanol by mono- and mixed cultures of bacteria". Appl Microbiol Biotechnol. 46 (5–6): 660–666. doi:10.1007/s002530050877. PMID 9008896. S2CID 43047193.
van Hylckama Vlieg JE, Tang LX, Lutje Spelberg JH, Smilda T, Poelarends GJ, Bosma T, van van Merode AE, Fraaije MW, Janssen DB (2001). "Halohydrin dehalogenases are structurally and mechanistically related to shortchain dehydrogenases/reductases". J Bacteriol. 183 (17): 5058–5066. doi:10.1128/jb.183.17.5058-5066.2001. PMC 95381. PMID 11489858.
You ZY, Liu ZQ, Zheng YG (2013). "Properties and biotechnological applications of halohydrin dehalogenases: current state and future perspectives". Appl Microbiol Biotechnol. 97 (1): 9–21. doi:10.1007/s00253-012-4523-0. PMID 23111599. S2CID 6884454.
Choi WJ, Choi CY (2005). "Production of chiral epoxides: epoxide hydrolase-catalyzed enantioselective hydrolysis". Biotechnol Bioprocess. 10 (3): 167–179. doi:10.1007/bf02932009. S2CID 84358740.
de Jong RM, Rozeboom HJ, Kalk KH, Tang LX, Janssen DB, Dijkstra BW (2002). "Crystallization and preliminary X-ray analysis of an enantioselective halohydrin dehalogenase from Agrobacterium radiobacter AD1". Acta Crystallogr D. 58 (Pt 1): 176–178. doi:10.1107/s0907444901019618. PMID 11752805.
de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2006). "The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family". J Bacteriol. 188 (11): 4051–4056. doi:10.1128/jb.01866-05. PMC 1482898. PMID 16707696.
de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2003). "Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site". EMBO J. 22 (19): 4933–4944. doi:10.1093/emboj/cdg479. PMC 204463. PMID 14517233.
Tang LX, Zhu XC, Zheng HY, Jiang RX, Elenkov MM (2012). "Key residues for controlling enantioselectivity of halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution". Appl Environ Microbiol. 78 (8): 4051–4056. Bibcode:2012ApEnM..78.2631T. doi:10.1128/AEM.06586-11. PMC 3318787. PMID 22327597.
Elenkov MM, Hauer B, Janssen DB (2006). "Enantioselective ring opening of epoxides with cyanide catalysed by halohydrin dehalogenases: a new approach to non-racemic β-hydroxy nitriles". Advanced Synthesis & Catalysis. 348 (4–5): 579–585. doi:10.1002/adsc.200505333.
Assis HM, Sallis PJ, Bull AT, Hardman DJ (1998). "Biochemical characterization of a haloalcohol dehalogenase from Arthrobacter erithii H10a. Enzyme". Enzyme Microb Technol. 22 (7): 568–574. doi:10.1016/s0141-0229(97)00254-8. PMID 9621448.

harvard.edu

ui.adsabs.harvard.edu

Tang LX, Zhu XC, Zheng HY, Jiang RX, Elenkov MM (2012). "Key residues for controlling enantioselectivity of halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution". Appl Environ Microbiol. 78 (8): 4051–4056. Bibcode:2012ApEnM..78.2631T. doi:10.1128/AEM.06586-11. PMC 3318787. PMID 22327597.

nih.gov

pubmed.ncbi.nlm.nih.gov

Fauzi AM, Hardman DJ, Bull AT (1996). "Biodehalogenation of low concentrations of 1,3-dichloropropanol by mono- and mixed cultures of bacteria". Appl Microbiol Biotechnol. 46 (5–6): 660–666. doi:10.1007/s002530050877. PMID 9008896. S2CID 43047193.
van Hylckama Vlieg JE, Tang LX, Lutje Spelberg JH, Smilda T, Poelarends GJ, Bosma T, van van Merode AE, Fraaije MW, Janssen DB (2001). "Halohydrin dehalogenases are structurally and mechanistically related to shortchain dehydrogenases/reductases". J Bacteriol. 183 (17): 5058–5066. doi:10.1128/jb.183.17.5058-5066.2001. PMC 95381. PMID 11489858.
You ZY, Liu ZQ, Zheng YG (2013). "Properties and biotechnological applications of halohydrin dehalogenases: current state and future perspectives". Appl Microbiol Biotechnol. 97 (1): 9–21. doi:10.1007/s00253-012-4523-0. PMID 23111599. S2CID 6884454.
de Jong RM, Rozeboom HJ, Kalk KH, Tang LX, Janssen DB, Dijkstra BW (2002). "Crystallization and preliminary X-ray analysis of an enantioselective halohydrin dehalogenase from Agrobacterium radiobacter AD1". Acta Crystallogr D. 58 (Pt 1): 176–178. doi:10.1107/s0907444901019618. PMID 11752805.
de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2006). "The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family". J Bacteriol. 188 (11): 4051–4056. doi:10.1128/jb.01866-05. PMC 1482898. PMID 16707696.
de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2003). "Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site". EMBO J. 22 (19): 4933–4944. doi:10.1093/emboj/cdg479. PMC 204463. PMID 14517233.
Tang LX, Zhu XC, Zheng HY, Jiang RX, Elenkov MM (2012). "Key residues for controlling enantioselectivity of halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution". Appl Environ Microbiol. 78 (8): 4051–4056. Bibcode:2012ApEnM..78.2631T. doi:10.1128/AEM.06586-11. PMC 3318787. PMID 22327597.
Assis HM, Sallis PJ, Bull AT, Hardman DJ (1998). "Biochemical characterization of a haloalcohol dehalogenase from Arthrobacter erithii H10a. Enzyme". Enzyme Microb Technol. 22 (7): 568–574. doi:10.1016/s0141-0229(97)00254-8. PMID 9621448.

ncbi.nlm.nih.gov

van Hylckama Vlieg JE, Tang LX, Lutje Spelberg JH, Smilda T, Poelarends GJ, Bosma T, van van Merode AE, Fraaije MW, Janssen DB (2001). "Halohydrin dehalogenases are structurally and mechanistically related to shortchain dehydrogenases/reductases". J Bacteriol. 183 (17): 5058–5066. doi:10.1128/jb.183.17.5058-5066.2001. PMC 95381. PMID 11489858.
de Jong RM, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2006). "The X-ray structure of the haloalcohol dehalogenase HheA from Arthrobacter sp. strain AD2: insight into enantioselectivity and halide binding in the haloalcohol dehalogenase family". J Bacteriol. 188 (11): 4051–4056. doi:10.1128/jb.01866-05. PMC 1482898. PMID 16707696.
de Jong RM, Tiesinga JJ, Rozeboom HJ, Kalk KH, Tang L, Janssen DB, Dijkstra BW (2003). "Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site". EMBO J. 22 (19): 4933–4944. doi:10.1093/emboj/cdg479. PMC 204463. PMID 14517233.
Tang LX, Zhu XC, Zheng HY, Jiang RX, Elenkov MM (2012). "Key residues for controlling enantioselectivity of halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution". Appl Environ Microbiol. 78 (8): 4051–4056. Bibcode:2012ApEnM..78.2631T. doi:10.1128/AEM.06586-11. PMC 3318787. PMID 22327597.

rug.nl

"Biodegradation of halogenated pollutants". 7 July 2011.

semanticscholar.org

api.semanticscholar.org

Fauzi AM, Hardman DJ, Bull AT (1996). "Biodehalogenation of low concentrations of 1,3-dichloropropanol by mono- and mixed cultures of bacteria". Appl Microbiol Biotechnol. 46 (5–6): 660–666. doi:10.1007/s002530050877. PMID 9008896. S2CID 43047193.
You ZY, Liu ZQ, Zheng YG (2013). "Properties and biotechnological applications of halohydrin dehalogenases: current state and future perspectives". Appl Microbiol Biotechnol. 97 (1): 9–21. doi:10.1007/s00253-012-4523-0. PMID 23111599. S2CID 6884454.
Choi WJ, Choi CY (2005). "Production of chiral epoxides: epoxide hydrolase-catalyzed enantioselective hydrolysis". Biotechnol Bioprocess. 10 (3): 167–179. doi:10.1007/bf02932009. S2CID 84358740.