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February 2018
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Cover Image
Cover Image
The X-ray crystal structure of the substrate binding pocket of cytochrome P450 enzyme CYP268A2, from Mycobacterium marinum, with the molecule pseudoionone bound in the active site. In this issue of the Biochemical Journal, Bell et al. show how the substrate becomes completely enclosed by the active site of the enzyme; for details see pages 705–722.
ISSN 0264-6021
EISSN 1470-8728
In this Issue
Editorial
Research Articles
Structural and functional characterisation of the cytochrome P450 enzyme CYP268A2 from Mycobacterium marinum
Biochem J (2018) 475 (4): 705–722.
Globular C1q receptor (p33) binds and stabilizes pro-inflammatory MCP-1: a novel mechanism for regulation of MCP-1 production and function
Biochem J (2018) 475 (4): 775–786.
Crystal structure of thermospermine synthase from Medicago truncatula and substrate discriminatory features of plant aminopropyltransferases
Biochem J (2018) 475 (4): 787–802.
Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase
Zhenbo Cao; Lorna Mitchell; Oliver Hsia; Miriam Scarpa; Stuart T. Caldwell; Arina D. Alfred; Alexandra Gennaris; Jean-François Collet; Richard C. Hartley; Neil J. Bulleid
Biochem J (2018) 475 (4): 827–838.