Zobrazeno 1 - 10
of 103
pro vyhledávání: '"V. Reiland"'
Publikováno v:
FEBS Journal. 274:3864-3876
The catalytic mechanism underlying the aminopeptidase from Streptomyces griseus (SGAP) was investigated. pH-dependent activity profiles revealed the enthalpy of ionization for the hydrolysis of leucine-para-nitroanilide by SGAP. The value obtained (3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b5faf6527ee8a74e8baacda9256f6c85
https://doi.org/10.1111/j.1742-4658.2007.05912.x
https://doi.org/10.1111/j.1742-4658.2007.05912.x
Autor:
Smadar Shulami, Larisa Rabinovitch, Yifat Fundoiano-Hershcovitz, Gil Shoham, Yuval Shoham, V. Reiland
Publikováno v:
FEMS Microbiology Letters. 243:157-163
The yet uncharacterized ywad gene from Bacillus subtilis has been cloned and overexpressed in Escherichia coli . The gene product (BSAP) was purified and shown to be an aminopeptidase. The activity of BSAP was optimal at pH 8.4, the enzyme was stable
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaa2296038b481b0e13ad2c09ae7ee07
https://doi.org/10.1016/j.femsle.2004.12.001
https://doi.org/10.1016/j.femsle.2004.12.001
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:2371-2376
The extracellular aminopeptidase from Bacillus subtilis (BSAP) has recently been cloned, overexpressed and purified from Escherichia coli. It is a monomer with a molecular weight of 46 425 Da, consisting of 425 amino-acid residues and a double-zinc c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7dd15045cbd2d0c446402b3448834a3
https://doi.org/10.1107/s0907444904026976
https://doi.org/10.1107/s0907444904026976
Autor:
Gil Shoham, Yuval Shoham, R. Gilboa, V. Reiland, Shmaryahu Blumberg, A. Spungin-Bialik, Dietmar Schomburg
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:1738-1746
The bacterial aminopeptidase isolated from the extracellular extract of Streptomyces griseus (SGAP) is a double-zinc exopeptidase with a high preference for large hydrophobic amino-terminus residues. It is a monomer of a relatively low molecular weig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73be86af1260c24161c3a527d9deb053
https://doi.org/10.1107/s0907444904018281
https://doi.org/10.1107/s0907444904018281
Autor:
V. Reiland, W. Frank
Publikováno v:
Acta Crystallographica Section C Crystal Structure Communications. 54:1626-1628
The title compound, [BiCl3(1,2,3-Me3C6H3)], contains quasi-dimeric units of arene-coordinated BiCl3 fragments that are further associated via additional Bi—Cl contacts to form coordination-polymeric layers. The resulting coordination number of Bi i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70467f39d5c4671a0d658eed1fb2f9d9
https://doi.org/10.1107/s0108270198008294
https://doi.org/10.1107/s0108270198008294
Autor:
A. Thompson, Gil Shoham, Adva Mechaly, Yuval Shoham, A. Teplitsky, V. Reiland, R. Gilboa, Vivian Stojanoff, Gali Golan, Gennady Zolotnitsky, G. Sainz, D. Shallom, H. Feinberg
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 60(Pt 5)
Xylanases are hemicellulases that hydrolyze the internal beta-1,4-glycoside bonds of xylan. The extracellular thermostable endo-1,4-beta-xylanase (EC 3.2.1.8; XT6) produced by the thermophilic bacterium Geobacillus stearothermophilus T-6 was shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c59be1c3346f4a00b17cf6c8f14bdb4
https://pubmed.ncbi.nlm.nih.gov/15103129
https://pubmed.ncbi.nlm.nih.gov/15103129
Autor:
Álvarez‐Martínez, Ignacio1,2 (AUTHOR), Ruprecht, Colin1,2 (AUTHOR), Senf, Deborah2 (AUTHOR), Wang, Hsin‐tzu3,4,5 (AUTHOR), Urbanowicz, Breeanna R.3,4 (AUTHOR), Pfrengle, Fabian1,2 (AUTHOR) fabian.pfrengle@boku.ac.at
Publikováno v:
Chemistry - A European Journal. 5/8/2023, Vol. 29 Issue 26, p1-8. 8p.
Autor:
Delano F 4th; Department of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, Michigan, 48824, USA., Demir S; Department of Chemistry, Michigan State University, 578 South Shaw Lane, East Lansing, Michigan, 48824, USA.
Publikováno v:
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2024 Oct 14, pp. e202417217. Date of Electronic Publication: 2024 Oct 14.
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