A. Clarke, D. Wigley, W. Chia, D. Barstow, T. Atkinson, and J. Holbrook. Site-directed mutagenesis reveals the role of a mobile arginine residue in lactate dehydrogenase catalysis. Nature, 324:699 -- 702, 1986. Home/Search Document Not in Database Summary Related Articles Check |
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Stochastic Roadmap Simulation: An Efficient.. - Apaydin, Brutlag, .. (2002) (5 citations) (Correct)
....A few amino acids are either deleted entirely or replaced by other amino acids, or alternatively, the side chains of amino acids are altered. Site directed mutagenesis has proven quite useful for many studies, including substrate recognition and identification of catalytic amino acids [CWC 86] The mutations made through this method are specific in terms of what changes are made, local in terms of exactly which amino acids are affected, and sound in terms of having no significant structural ramifications. Computational mutagenesis embodies these concepts from site directed ....
....in its bound conformation in the LDH NADH substrate complex is depicted in Figure 10. The amino acids that play a significant role in the catalytic activity of the enzyme are shown. Arg169 assists in orienting and binding the substrate [HCW 87] Arg106 polarizes the carbonyl bond on the substrate [CWC 86] His193 is an important catalytic residue, which donates a proton to the substrate during its reduction [HLSR75] His193 is then stabilized by Asp166 [CBA 88] In native LDH, before the binding of the coenzyme or the substrate, a loop of polypeptide chain (residues 97 to 107) is positioned away ....
A. Clarke, D. Wigley, W. Chia, D. Barstow, T. Atkinson, and J. Holbrook. Site-directed mutagenesis reveals the role of a mobile arginine residue in lactate dehydrogenase catalysis. Nature, 324:699 -- 702, 1986.
Stochastic Roadmap Simulation: An efficient.. - Apaydin, Brutlag, .. (2002) (5 citations) (Correct)
No context found.
A. Clarke, D. Wigley, W. Chia, D. Barstow, T. Atkinson, and J. Holbrook. Site-directed mutagenesis reveals the role of a mobile arginine residue in lactate dehydrogenase catalysis. Nature, 324:699 -- 702, 1986.
Bioinformatics - Vol No Pages (2002) (Correct)
No context found.
A. Clarke, D. Wigley, W. Chia, D. Barstow, T. Atkinson, and J. Holbrook. Site-directed mutagenesis reveals the role of a mobile arginine residue in lactate dehydrogenase catalysis. Nature, 324:699 -- 702, 1986.
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