what is turn over number?
- 4 Answers
- 23363 Views
- Aurobindo, I also Faced
- E-Mail Answers
Answers were Sorted based on User's Feedback
Answer / abhilash
The catalytic power of anenzyme is measured by the "turn
over number" or molecular activity.
it is defined as the number of substrate molecules
converted into product per unit time ,when the enzyme is
fully saturated with substrate.
for example catalase can convert 5,000,000 times its own
weight of H2O2 into H20 and O2.
the value of turn over number varies with different enzymes
and depends upon the conditions in which the reaction is
taking place.
most of the turnover numbers fall between 1 to 10 powers 4.
| Is This Answer Correct ? | 45 Yes | 10 No |
Answer / dr.shaukat saeed khan
It is equivalent to Vmax being the number of substrate
molecules converted to product by one enzyme molecule in
unit time(often 1 second)when there is saturation of the
substrate. Mathematically it can be expressed as
Kcat=Vmax/Et,
where Kcat=Turn over number
Vmax=Maximum rate of reaction when all the active sites of
the enzyme are saturated with the specific substrate
Et=Total enzyme concentration or the concentration of
active sites of the enzyme.
The turn over number differs from enzyme to enzyme under
identical experimental conditions and under different
conditions for the same enzyme.
| Is This Answer Correct ? | 10 Yes | 2 No |
Answer / lukas
Besides the describing the enzyme activity, TON is also used
in an organometalic catalysis. Here, nevertheless, TON has
slightly different meaning. TON describes how many catalitic
cycles catalyst undergoes before it dies. In other words,
How many moles of substrate is converted by one mol of
catalys. here TON is NOT related to the unit of time. When
the TON is related to the unit of time, the term Turn Over
Frequency (TOF) is used instead.
| Is This Answer Correct ? | 6 Yes | 0 No |
Answer / peter
Turn over numbr also known as Kcat, is defined as the
maximum number of substrate molecules that can an enzyme
converted to products per catalytic site per (unit time)
seconds, and can mathematically also be defined as Kcat =
Vmax/[Et]* (sec). Vmax denote maximum velocity at which the
enzyme active site is saturated with increasing substrate
concentration, Kcat denote catalytic constant, and [Et]m
denote enzyme total concentration.
| Is This Answer Correct ? | 5 Yes | 2 No |
What are babes Ernst granules?
Because of dna replication, two dna molecules come to existence. Why is not it correct to assert that two “new” dna molecules are created? What is the name given to the process concerning that fact?
what is reichert-meissl number?
What is Co-ordination number?
How immunoglobulin fold looks like?
Where is csf found?
DNA binding by proteins with the helix-turn-helix (HTH) motif does not involve a) altered stacking of the DNA at the center of symmetry. b) hydrogen bonds, salt bridges, and van der Waals contacts. c) interactions with base pairs in the major groove of DNA. d) interactions with the sugar-phosphate backbone of DNA.
The junction between the two helical portions of tRNA is stabilized by many non-standard base-base interactions between residues in the a) anticodon and CCA ends. b) helical stems of the D and Anticodon stems. c) loops of the Anticodon and Acceptor stem. d) loops of the TYC and D arms.
I have given the protocol for the cyclodextrin glygosyl transferase assay: One ml of appropriately diluted enzyme sample was incubated at 60 °C for 15 min with 5 ml of 1% (w/v) gelatinized soluble starch in 50 mM, 7.0-pH Tris–HCl buffer. Reaction was terminated by boiling the reaction mixture for 3 min and reaction volume was made to 10 ml with distilled water. Two ml of above reaction mixture was withdrawn and mixed with 3 ml of Tris–HCl buffer, 5 ml of 125 mM Na2CO3, and 0.5 ml of phenolphthalein (25 mg phenolphthalein/100 ml absolute alcohol). Absorbance was measured at 550 nm. The percent decrease of sample was calculated with respect to control containing 5 ml of buffer, 5 ml of sodium carbonate and 0.5 ml of phenolphthalein. where Acontrol = absorbance of control and Atest = absorbance of sample. The amount of β-cyclodextrin (β-CD) produced was estimated from the standard graph of 0–500 μg/ml β-CD concentration against % decrease in absorbance. One unit of CGTase was defined as the amount of enzyme required to produce 1 μm of β-CD/min. Please can you suggest me the formula for the defination given in the last line
How can proteins be denatured and renatured?
How are free energy changes related to LeChatelier's Principle?
Who proposed law of mass action?
Micro Biology 
