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pro vyhledávání: '"Karl A.P. Payne"'
Autor:
Shalini Iyer, Penelope J. La-Borde, Karl A.P. Payne, Mark R. Parsons, Anthony J. Turner, R. Elwyn Isaac, K. Ravi Acharya
Publikováno v:
FEBS Open Bio, Vol 5, Iss 1, Pp 292-302 (2015)
Eukaryotic aminopeptidase P1 (APP1), also known as X‐prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N‐terminus of peptides possessing a penultimate N‐terminal proli
Externí odkaz:
https://doaj.org/article/a81b952de5dc4dc08fa330f7521a86c9
Publikováno v:
Gahloth, D, Fisher, K, Payne, K A P, Cliff, M, Levy, C & Leys, D 2022, ' Structural and biochemical characterisation of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase ', Journal of Biological Chemistry, pp. 101771 . https://doi.org/10.1016/j.jbc.2022.101771
The ubiquitous UbiD family of reversible decarboxylases is implicated in a wide range of microbial processes and depends on the prenylated flavin mononucleotide (prFMN) cofactor for catalysis. However, only a handful of UbiD family members have been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c34cebc3155e2a1c0847b69ed09453d
https://www.research.manchester.ac.uk/portal/en/publications/structural-and-biochemical-characterisation-of-the-prenylated-flavin-mononucleotidedependent-indole3carboxylic-acid-decarboxylase(1a645aa3-def4-4286-9fcc-5bca1aa0a7f5).html
https://www.research.manchester.ac.uk/portal/en/publications/structural-and-biochemical-characterisation-of-the-prenylated-flavin-mononucleotidedependent-indole3carboxylic-acid-decarboxylase(1a645aa3-def4-4286-9fcc-5bca1aa0a7f5).html