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Active-site architecture

The crystal structure of the HNL isolated from S. bicolor (SbHNL) was determined in a complex with the inhibitor benzoic acid." The folding pattern of SbHNL is similar to that of wheat serine carboxypeptidase (CP-WII)" and alcohol dehydrogenase." A unique two-amino acid deletion in SbHNL, however, is forcing the putative active site residues away from the hydrolase binding site toward a small hydrophobic cleft, thereby defining a completely different active site architecture where the triad of a carboxypeptidase is missing. [Pg.151]

DAVIES, C., HEATH, R.J., WHITE, S.W., ROCK, C.O., The 1.8 A crystal structure and active-site architecture of P-ketoacyl-acyl carrier protein synthase HI (FabH) from Escherichia coli, Structure, 2000, 8, 185-195. [Pg.220]

Sulzenbacher, G., Gal, L., Peneff, C., Fassy, F., and Bourne, Y. (2001). Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyl transferase bound to acetyl-coenzyme A reveals a novel active site architecture. J. Biol. Chem. 276, 11844-11851. [Pg.96]

Fig. 6. The active site architecture of eNOS in the A subunit. L-Arg is held in place by several H-bonds with conserved groups. The H4B is sandwiched between aromatic groups contributed from each subunit Trp449 in subunit A and Phe462 in subunit B. Note that the amino group of L-Arg and the pterin donate an H-bond to the same heme propionate, which helps to understand the observed interdependence of pterin and substrate binding. The schematic diagram illustrates the extensive contacts between pterin and protein groups in each subunit. Fig. 6. The active site architecture of eNOS in the A subunit. L-Arg is held in place by several H-bonds with conserved groups. The H4B is sandwiched between aromatic groups contributed from each subunit Trp449 in subunit A and Phe462 in subunit B. Note that the amino group of L-Arg and the pterin donate an H-bond to the same heme propionate, which helps to understand the observed interdependence of pterin and substrate binding. The schematic diagram illustrates the extensive contacts between pterin and protein groups in each subunit.
Rupasinghe, S., Baudry, J., and Schuler, M.A., Common active site architecture and binding strategy of four phenylpropanoid P450s from Arabidopsis thaliana as revealed by molecular modeling. Prot. Eng., 16, 721, 2003. [Pg.202]

Ribas dePoplana L, Fothergill-Gilmore LA. The active site architecture of a short chain dehydrogenase defined by site-directed mutagenesis and structure modeling. Biochemistry 33 1994 7047-7055. [Pg.210]

Active-site architecture retained In this case, the active site is able to support alternative reactions with shared functional groups in a different mechanistic or metabolic context.The study of a/jS-barrel proteins, also termed ()3a)8-barrel... [Pg.457]

Rutten, L., Mannie, J.P., Stead, C.M., Raetz, C.R., Reynolds, C.M., Bonvin, A.M., Tommassen, J.P., Egmond, M.R., Trent, M.S., Gros, P. Active-site architecture and catalytic mechanism of the lipid A deacylase LpxR of Salmonella typhimurium. Proc Natl Acad Sci USA 106 (2009)... [Pg.25]

Figure 1 (a) Schematic representation of yeast cytochrome c peroxidase (CcP) structure with heme and key active site residues represented as ball-and-stick models, (b) Active site architecture of yeast cytochrome c peroxidase (CcP) showing the role of all the key residues in catalysis. The dashed lines represent hydrogen bonds... [Pg.1938]

The mid-chain dehydrogenation of saturated fatty acyl derivatives is carried out by a large family of 02-dependent, nonheme diiron-containing enzymes known as desaturases. Both soluble and membrane-bound desaturases have been characterized. The mechanism of desaturation is thought to involve the stepwise syn removal of vicinal hydrogen atoms via a short-lived carbon-centered radical intermediate. The most common desaturase inserts a (Z)-double bond between the C-9,10 carbons of a stearoyl thioester however, many variations of this prototypical reaction have been discovered. Accounting for this diversity in terms of subtle alterations in active-site architecture constitutes a new frontier for research in this area. [Pg.493]

Phosphonamidothioates show strong promise as potent tetrahedral-inter-mediate analogue inhibitors of metallopeptidases, with the unique value of probing enzyme active site architecture with complementary chiral phosphorus... [Pg.177]

The active site architecture of flavocytochrome 62 (25) is very similar to that seen in glycolate oxidase (54), with residues equivalent to those mentioned above presumably performing equivalent functions in the latter enzyme. [Pg.267]

Davies, C., Heath, R. I., White. 3. W.. and Rock, C. O. 2000. The l. A crystal structure and active site architecture of p-kctoacyl-acyl carrier protein synthase 111 (EabH) from Eschen t/iiu co i. StrudurcfoM... [Pg.646]


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