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Alanine residues dehydrogenases

Alanine residues, glyceraldehyde-3-phos-phate dehydrogenase, 11,12 Alcohols, catalase smd, 388, 398, 401 Aldehydes, glyceraldehyde-3-phosphate dehydrogenase smd, 39 Algae, sulfate assimilation by, 279, 280 Alkali... [Pg.436]

Figure 6a shows the modeled oc helix F interface in human 17 3-hydroxysteroid dehydrogenase type 1 in which phenylalanine-160 and alanine-161 form an anchor. Both residues have important stabilizing interactions across the dimer interface. Alanine-161 is 4.1 A from alanine-161 on the other subunit. Alanine-161 has a hydrophobic interaction with alanine-157, which is in the segment between the conserved tyrosine-155 and lysine-159. There is a hydrophobic... [Pg.205]

Figure 6b shows the modeled a helix F interface in human 17P-hydroxysteroid dehydrogenase type 2. Alanine-237 is 3 A from the hydrophobic part of the side chain of methionine-241 on the other subunit. Methionine-241 is 3.2 A from serine-234. Alanine-230 is 3.7 A from phenylalanine-242 and 4.5 A from valine-245. Alanine-238, the other anchoring residue, is 4.1 A from alanine-238 on the other subunit. [Pg.206]

See other pages where Alanine residues dehydrogenases is mentioned: [Pg.101]    [Pg.203]    [Pg.206]    [Pg.775]    [Pg.796]    [Pg.775]    [Pg.796]    [Pg.140]    [Pg.431]    [Pg.285]    [Pg.137]    [Pg.679]    [Pg.137]    [Pg.179]    [Pg.196]    [Pg.311]   
See also in sourсe #XX -- [ Pg.88 ]



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Alanine residues

Dehydrogenases alanine dehydrogenase

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