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pro vyhledávání: '"Emma S.V. Andrews"'
Autor:
Vickery L. Arcus, Emma S.V. Andrews
Publikováno v:
Protein Sci
PhoH2 proteins are found in a very diverse range of microorganisms that span bacteria and archaea. These proteins are composed of two domains: an N‐terminal PIN‐domain fused with a C‐terminal PhoH domain. Collectively this fusion functions as a
Publikováno v:
PLoS ONE, Vol 15, Iss 7, p e0236551 (2020)
PLoS ONE
PLoS ONE
PhoH2 proteins are highly conserved across bacteria and archaea yet their biological function is poorly characterised. We examined the growth profiles of Mycobacterium smegmatis strains mc2155 and mc2155 ΔphoH2 and observed the same growth profile a
Publikováno v:
Analytica Chimica Acta. 1156:338218
Malic acid is a key flavour component of many fruits and vegetables. There is significant interest in technologies for monitoring its concentration, particularly in winemaking. In this review we systematically and comprehensively chart progress in th
Autor:
David J. Leak, Michael J. Danson, Vickery L. Arcus, Susan J. Crennell, Emma S.V. Andrews, Lisa Buddrus
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
Buddrus, L, Andrews, E S V, Leak, D J, Danson, M J, Arcus, V L & Crennell, S J 2016, ' Crystal structure of pyruvate decarboxylase from Zymobacter palmae ', Acta Crystallographica Section F:Structural Biology Communications, vol. 72, no. 9, pp. 700-706 . https://doi.org/10.1107/S2053230X16012012
Buddrus, L, Andrews, E S V, Leak, D J, Danson, M J, Arcus, V L & Crennell, S J 2016, ' Crystal structure of pyruvate decarboxylase from Zymobacter palmae ', Acta Crystallographica Section F:Structural Biology Communications, vol. 72, no. 9, pp. 700-706 . https://doi.org/10.1107/S2053230X16012012
The crystal structure of Z. palmae pyruvate decarboxylase was elucidated at 2.15 Å resolution.
Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg2+ ion-dependent enzyme that catalyses the non-oxidative decarboxylation
Pyruvate decarboxylase (PDC; EC 4.1.1.1) is a thiamine pyrophosphate- and Mg2+ ion-dependent enzyme that catalyses the non-oxidative decarboxylation
Publikováno v:
PLoS ONE, Vol 13, Iss 8, p e0203412 (2018)
The chromosome of Mycobacterium tuberculosis (Mtb) contains a large number of Type II toxin-antitoxin (TA) systems. The majority of these belong to the VapBC TA family, characterised by the VapC protein consisting of a PIN domain with four conserved
Autor:
Emma S.V. Andrews, Vickery L. Arcus
Publikováno v:
Tuberculosis (Edinburgh, Scotland). 95(4)
Summary PhoH2 proteins are found in a diverse range of organisms that span the bacterial tree and little is known about this large protein family. PhoH2 proteins have two domains: An N-terminal PIN domain fused to a C-terminal PhoH domain. The genome
Autor:
Peter J. Myler, Jan Abendroth, Emma S.V. Andrews, Christoph Grundner, Anja R Ollodart, Bart L. Staker, Vickery L. Arcus, Thomas E. Edwards
Publikováno v:
The Journal of biological chemistry. 289(4)
Ribonucleases (RNases) maintain the cellular RNA pool by RNA processing and degradation. In many bacteria, including the human pathogen Mycobacterium tuberculosis (Mtb), the enzymes mediating several central RNA processing functions are still unknown