Results 71 to 80 of about 365,538 (313)
High coenzyme affinity chimeric amine dehydrogenase based on domain engineering
Bioresources and Bioprocessing, 2022 NADH-dependent phenylalanine amine dehydrogenase (F-AmDH) engineered from phenylalanine dehydrogenase (PheDH) catalyzes the synthesis of aromatic chiral amines from prochiral ketone substrates.
Jialin Li, Xiaoqing Mu, Tao Wu, Yan Xu
doaj +1 more source
, 2023 While the reverse water-gas shift (RWGS) reaction holds great promise as a method of converting CO2 to CO and subsequently into valuable fuels, achieving its commercial viability requires the development of highly efficient, selective, durable, and low ...
Veronika Nagy-Trembošová +5 more
core +1 more source
FEBS Letters, EarlyView.We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee +3 more
wiley +1 more source
Journal of Lipid Research, 2018 Delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for PUFA biosynthesis. In some organisms, FADS2s have high substrate specificity, whereas in others, they have high catalytic activity. Previously, we analyzed the molecular mechanisms
Haisu Shi +7 more
doaj +1 more source
FEBS Letters, EarlyView.Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes +4 more
wiley +1 more source
Selective replacement of the catalytic zinc of the human stromelysin-1 catalytic domain [PDF]
JBIC Journal of Biological Inorganic Chemistry, 1998 We have selectively replaced the catalytic zinc of the catalytic domain of stromelysin-1 (SCD) with other transition metals. Dialysis of the enzyme against 2 mM 1,10-phenanthroline, 20 mM Hepes, pH 7.5 in the presence of 10 mM CaCl2 removes the catalytic zinc, leaving the structural zinc site intact.
Jaeho Cha +3 more
openaire +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
FEBS Letters, EarlyView.Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source
Future Science OAProtein kinases are vital drug targets, yet designing selective inhibitors is challenging, compounded by resistance and kinome complexity. This review explores Quantitative Structure-Activity Relationship (QSAR) modeling for kinase drug discovery ...
Rand Shahin, Sawsan Jaafreh, Yusra Azzam
doaj +1 more source
Rethinking Leucine Zipper : ribonuclease activity and structural dynamics of a ubiquitous oligomerization motif [PDF]
, 2011 This dissertation focuses on structural, dynamic and catalytic properties of a Leucine Zipper (LZ) motif – a family of protein oligomerization domains which belong to the structural class of coiled coil proteins.
Nikolaev, Yaroslav
core +1 more source
Structural insights into an engineered feruloyl esterase with improved MHET degrading properties
FEBS Letters, EarlyView.A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa +5 more
wiley +1 more source