Biochem please help am so lost Ill rate The following sequen

Biochem please help am so lost I\'ll rate!

The following sequence alignment between several species shows many conserved residues that may take part in the catalytic function.

1. The mutants R292G and R292A of the Ar-BVMO monooxygenase enzyme showed very small residual activities compared to the wild-type enzyme. What is the catalytic role of this arginine residue considering the enzyme reaction mechanism?

1. The mutants R292G and R292A of the Ar-BVMO monooxygenase enzyme showed very small residual activities compared to the wild-type enzyme. What is the catalytic role of this arginine residue considering the enzyme reaction mechanism?
131 140 170 190 VOSRROPPEEVOVL MSTFGYNI AINR EILERRESEGGIWOLFR EGETINTRRI ATRITL EIE RTRITL RINA EIE VIGSE d..E 410 430 Ar-Ivno RNIGORRWYRLsao----------------------- KNWLRONINYSRCual----------------------------- 690693 620 210 EQIREIKROTORINE TIILORSPITIRSI- PS ITIVSQ------PDRDGIRE 510 WRONGTWISTL .ple..T 610

Solution

Answer:

Baeyer–Villiger monooxygenases (BVMOs) form a distinct class of flavoproteins that catalyze the insertion of an oxygen atom in a C–C bond using dioxygen and NAD(P)H.

Ar-BVMO is a recently discovered Baeyer-Villiger monooxygenase from the genome of Acinetobacter radioresistens Experiments performed by Site-directed mutagenesis decipher the role of the active site arginine-292.

Replacement of arginine 292 in Ar-BVMO by glycine or alanine resulted in greatly reduced when by glycin and no Baeyer-Villiger activity when replaced by alanin,

The active site Arginine 292 is required for its Baeyer-Villiger activity but not for heteroatom oxidation.

A single mutation converts Ar-BVMO to a unique S- or N-monooxygenase, a useful biocatalyst for the production of oxidized metabolites of human drug metabolizing enzymes.

Biochem please help am so lost I\'ll rate! The following sequence alignment between several species shows many conserved residues that may take part in the cata

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