Kinetic and Chemical Mechanism of ArylamineN-Acetyltransferase fromMycobacterium tuberculosis†

Kinetic mechanism of the histone acetyltransferase GCN5 from yeast.

The transcriptional coactivator GCN5 from yeast (yGCN5) is a histone acetyltransferase that is essential for activation of target genes. GCN5 is a member of a large family of histone acetyltransferases that are conserved between yeast and humans. To understand the molecular mechanisms of histone/protein acetylation, a detailed kinetic analysis was performed. Bi-substrate kinetic analysis using ...

The kinetic mechanism of kanamycin acetyltransferase derived from the use of alternative antibiotics and coenzymes.

Kinetic data for the 6'-aminoglycoside-modifying enzyme, AAC(6')-4, also named kanamycin acetyltransferase, have been collected for six aminoglycoside antibiotics (amikacin, gentamicin C1a, kanamycin A, neomycin B, sisomicin, and tobramycin) and three coenzymes (acetyl-CoA, n-propionyl-CoA, and n-butyryl-CoA). The initial velocity pattern using acetyl-CoA favors a ping-pong kinetic mechanism (K...

extraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties

آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...

Re-evaluation of the kinetic mechanism of the choline acetyltransferase reaction.

Initial velocity patterns for human placental choline acetyltransferase show a series of converging lines for both the forward and reverse reaction; with Kacetyl coenzyme A = 11.9 micron, Kcholine = 0.41 mM, KCOA = 8.8 micron, and Kacetylcholine = 1.3 mM. The relative rates of acetylcholine synthesis (Vf) to acetylcholine breakdown (Vr) is 4.5. Product inhibition by acetylcholine is competitive...

PCAF Histone Acetyltransferase Processing of a Peptide Substrate: Kinetic Analysis of the Catalytic Mechanism*