Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Robert C. Bruckner"'
Publikováno v:
Biochemistry. 50:4949-4962
N-Methyltryptophan oxidase (MTOX) contains covalently bound FAD. N-Methyltryptophan binds in a cavity above the re face of the flavin ring. Lys259 is located above the opposite, si face. Replacement of Lys259 with Gln, Ala, or Met blocks (95%) covale
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9133119e9cbe96d917f8fc0e0b9069de
https://doi.org/10.1021/bi200349m
https://doi.org/10.1021/bi200349m
Autor:
Marilyn Schuman Jorns, Robert C. Bruckner, Phaneeswara Rao Kommoju, F. Scott Mathews, Patricia Ferreira, Christopher J. Carrell
Publikováno v:
Biochemistry. 48:9542-9555
NikD is a flavoprotein oxidase that catalyzes the oxidation of piperideine-2-carboxylate (P2C) to picolinate in a remarkable aromatization reaction comprising two redox cycles and at least one isomerization step. Tyr258 forms part of an "aromatic cag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::052dbf2a253598f6f5c24adf37f9347f
https://doi.org/10.1021/bi901056a
https://doi.org/10.1021/bi901056a
Publikováno v:
Biochemistry. 48:4455-4465
NikD is a flavoprotein oxidase that plays an essential role in the biosynthesis of nikkomycins. Nikkomycins comprise a group of related peptidyl nucleoside antibiotics that resemble the natural substrate of chitin synthase. Chitin, the second most ab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::313655717d361e7862928d17b6650191
https://doi.org/10.1021/bi900179j
https://doi.org/10.1021/bi900179j
Publikováno v:
Biochemistry. 47:9124-9135
Monomeric sarcosine oxidase (MSOX) catalyzes the oxidation of N-methylglycine and contains covalently bound FAD that is hydrogen bonded at position N(5) to Lys265 via a bridging water. Lys265 is absent in the homologous but oxygen-unreactive FAD site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e96f68b9685390b7ea745d58e663d1b9
https://doi.org/10.1021/bi8008642
https://doi.org/10.1021/bi8008642
Autor:
Marilyn Schuman Jorns, David Venci, F. Scott Mathews, Christopher J. Carrell, Gouhua Zhao, Robert C. Bruckner
Publikováno v:
Structure. 15(8):928-941
NikD is an unusual amino-acid-oxidizing enzyme that contains covalently bound FAD, catalyzes a 4-electron oxidation of piperideine-2-carboxylic acid to picolinate, and plays a critical role in the biosynthesis of nikkomycin antibiotics. Crystal struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21be3a2339a463f3a3c56aa3a32b609c
Autor:
Robert C. Bruckner, Andrew M. Stern, Anne Higley, Graciani Nilsa R, Sandya Mandlekar, Maria Rafalski, Melody Diamond, Ross L. Stein, Eddy W. Yue, Xiang Jiang, Pearl S. Huang, Randine Dowling, Dimeo Susan, Lisa C. Grimminger, Mingzhu Zhang, Zhihong Lai, Amy L. Musselman, Swamy Yeleswaram, Davette L. Behrens, Robert A. Copeland, Andrew P. Combs, Oliff Allen I, Wei Han, Shu-Yun Zhang, Rebecca Taub, Bruce Car, George L. Trainor, Charles F. Albright, Steve P. Seitz, Daniel Hu
Publikováno v:
Molecular Cancer Therapeutics. 4:751-760
Matrix metalloproteinase (MMP)–activated prodrugs were formed by coupling MMP-cleavable peptides to doxorubicin. The resulting conjugates were excellent in vitro substrates for MMP-2, -9, and -14. HT1080, a fibrosarcoma cell line, was used as a mod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45501a8fa2fc432573f20a1fa75bdc1c
https://doi.org/10.1158/1535-7163.mct-05-0006
https://doi.org/10.1158/1535-7163.mct-05-0006
Publikováno v:
Biochemistry. 44:6452-6462
The covalently bound FAD in native monomeric sarcosine oxidase (MSOX) is attached to the protein by a thioether bond between the 8alpha-methyl group of the flavin and Cys315. Large amounts of soluble apoenzyme are produced by controlled expression in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bcc880693b0e801ba8efb06be6815b4
https://doi.org/10.1021/bi047271x
https://doi.org/10.1021/bi047271x
Autor:
Zhiwei Chen, Phaneeswara Rao Kommoju, Robert C. Bruckner, F. Scott Mathews, Marilyn Schuman Jorns
Publikováno v:
Biochemistry. 50(24)
A single basic residue above the si-face of the flavin ring is the site of oxygen activation in glucose oxidase (GOX) (His516) and monomeric sarcosine oxidase (MSOX) (Lys265). Crystal structures of both flavoenzymes exhibit a small pocket at the oxyg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2388245364da5538823fd4c009257bd6
https://pubmed.ncbi.nlm.nih.gov/21568312
https://pubmed.ncbi.nlm.nih.gov/21568312
Publikováno v:
Proceedings of the National Academy of Sciences. 89:10950-10954
We have partially purified an activity from extracts of cells infected with herpes simplex virus type 1 that mediates recombination between repeated copies of the 317-base-pair a sequence of herpes simplex virus type 1. Recombination leads to deletio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6257fef25d8e64f511103e9ba1bd443
https://doi.org/10.1073/pnas.89.22.10950
https://doi.org/10.1073/pnas.89.22.10950
Publikováno v:
Journal of Virology. 66:277-285
During the course of infection, elements of the herpes simplex virus type 1 (HSV-1) genome undergo inversion, a process that is believed to occur through the viral a sequences. To investigate the mechanism of this recombinational event, we have devel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac47494c9548e482c1e6d63fb4e0564f
https://doi.org/10.1128/jvi.66.1.277-285.1992
https://doi.org/10.1128/jvi.66.1.277-285.1992