Year: 1996
Type: article
Abstract: MACROMOLECULES(residues !39-!322 and !3275-!3295) is missing in OASS.There are two additional smface helices in TRPSJ3 (residues !323-1354) and an additional loop (!3260-13266).The active site cleft of OASS is wider and therefore more exposed to the solvent.The hydrophobic channel for indole transport from the a to the J3 active site is, not unexpectedly, missing in OASS.The dimer interface, however, is more or less conserved in the two enzymes.The only cysteine residue of OASS (which is the residue following the active site lysine in the sequence) cannot be directly involved in the reaction mechanism, since it is completely buried and more than I 0 A away from the PLP cofactor.Further investigations on substrate binding and possible reaction mechanisms are planned.
Authors: A. Johnson, V. Pattabhi, P. V. Sundaram
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2324497108