Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Matthias E. Henz"'
Autor:
Rainer Martin Lüönd, Peter Schürmann, Caroline Jarret, Maurus Marty, Janette Bobalova, Reinhard Neier, Matthias E. Henz, Frédéric Stauffer
Publikováno v:
Chemistry & Biology. 7:185-196
Background: Porphobilinogen synthase is the second enzyme involved in the biosynthesis of natural tetrapyrrolic compounds, and condenses two molecules of 5-aminolevulinic acid (ALA) through a nonsymmetrical pathway to form porphobilinogen. Each subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7669cb24fab328bed33601ed38a80c3
https://doi.org/10.1016/s1074-5521(00)00089-2
https://doi.org/10.1016/s1074-5521(00)00089-2
Autor:
Marion Kirk, Kathleen A. Merkler, Uta Glufke, Lawrence King, John C. Vederas, Benjamin J. Wilcox, David J. Merkler, Stephen Barnes, Matthias E. Henz
Publikováno v:
Archives of Biochemistry and Biophysics. 374:107-117
Bifunctional peptidylglycine α-amidating monooxygenase (PAM) catalyzes the copper-, ascorbate-, and O 2 -dependent cleavage of C-terminal glycine-extended peptides and N -acylglycines to the corresponding amides and glyoxylate. The α-amidated pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a02831dba17ba8264398a91ef9a44db7
https://doi.org/10.1006/abbi.1999.1611
https://doi.org/10.1006/abbi.1999.1611
Autor:
Liang Z. Yan, John C. Vederas, David S. Wishart, Yunjun Wang, Matthias E. Henz, Michael E. Stiles, Nancy L. Fregeau Gallagher, Shengyong Chai, Alan C. Gibbs
Publikováno v:
Biochemistry. 38:15438-15447
Carnobacteriocin B2 (CbnB2), a type IIa bacteriocin, is a 48 residue antimicrobial peptide from the lactic acid bacterium Carnobacterium pisicola LV17B. Type IIa bacteriocins have a conserved YGNGVXC sequence near the N-terminus and usually contain a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b9e4cc407008c24f57386cbaaf81dba
https://doi.org/10.1021/bi991351x
https://doi.org/10.1021/bi991351x
Autor:
Alexander S. Asser, Lawrence King, John J. Robleski, Benjamin J. Wilcox, Megan A. Baumgart, Matthias E. Henz, Kimberly J. Ritenour-Rodgers, Laura E. Baumgart, Uta Glufke, Mitchell A. deLong, Dale L. Boger, Kathleen A. Merkler, Jean E. Patterson, David J. Merkler, Jodi L. DeBlassio, John C. Vederas
Publikováno v:
Biochemistry. 38:3235-3245
Bifunctional peptidylglycine alpha-amidating enzyme (alpha-AE) catalyzes the O2-dependent conversion of C-terminal glycine-extended prohormones to the active, C-terminal alpha-amidated peptide and glyoxylate. We show that alpha-AE will also catalyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c66c32ff42c9ce640adc3700d5860e2
https://doi.org/10.1021/bi982255j
https://doi.org/10.1021/bi982255j