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Oracle reduces the potential impact of contention in two basic ways The first way is to reduce the scope of locks and the overhead required to manage those locks The atomic unit for standard I/O operations in the Oracle database is the block All standard reads from and writes to Oracle data access at least one block of data Blocks are typically 2 to 32KB, so each block usually contains multiple data rows Despite this fact, Oracle does not place locks on an entire block of data, which would result in having some rows that were not being modified or read being locked This feature is called row-level locking Oracle is certainly not unique in this approach, as many modern, robust databases also lock at the row level Most other databases use a lock manager to hold active locks and to limit access to rows based on these locks Having row-level locks can result in a lot of locks being used by the database, which can mean a lot of resources used by the lock manager For this reason, some other databases have a policy of lock escalation Lock escalation occurs when the overhead of managing a lot of row-level locks becomes resource intensive, so the lock manager converts a group of locks on one entity to a single lock on a larger entity For instance, if the lock manager detects that a significant percentage of rows in a block are locked, it would release the row-level locks and place a lock on the block If many blocks were locked, a lock manager could swap these locks for a lock with a larger scope, such as a table In these cases, the efficient route for the lock manager can have the effect of increasing contention and reducing overall throughput The Oracle database avoids this problem by removing the lock manager from the overall process Instead of storing locks in a lock manager, Oracle simply stores locks in the same block as the data being locked Since a data.

This modification is not directly reversible, but the phosphate group can be removed from the protein by the action of protein phosphatases Protein O PO2 3 H2O Protein OH Pi Phosphorylation activates some proteins and inactivates others The actual phosphorylation of a regulated protein is often catalyzed by a protein kinase that is specific for one or just a few proteins; however, the protein kinases themselves are often regulated by phosphorylationdephosphorylation mechanisms At least for the regulatory enzymes of energy metabolism, the thing that usually starts the whole phosphorylation mess is cAMP-dependent protein kinase This enzyme is activated by increases in the levels of cAMP, a second messenger for low-energy and low-glucose levels Activation of cAMP-dependent protein kinase ultimately leads to increased protein phosphorylation For example, phosphorylation of phosphorylase, the enzyme responsible for degrading glycogen to glucose 1-phosphate, activates the enzyme Glycogen degradation in both liver and muscle is required under low-glucose or low-energy conditions, conditions associated with increased protein phosphorylation In contrast, glycogen synthase, which must be turned off under conditions of low glucose levels, is inactivated by phosphorylation The easy way to decide if phosphorylation activates or inactivates a given enzyme is to decide whether the pathway that uses the enzyme should be on or off under conditions favoring phosphorylation (low energy or low glucose) If the pathway should be on under low-energy or low-glucose conditions, phosphorylation should activate the pathway and the enzyme in question If the pathway should be off, phosphorylation should inactivate the enzyme Phosphorylase is simple enough, and the regulation of most other enzymes can be figured out using the principle outlined earlier The following example taken from the regulation of glycolysis and gluconeogenesis, is probably the most complicated one you ll see How does phosphorylation affect the activity of phosphofructo-2kinase (PFK-2), the enzyme that synthesizes fructose 2,6-bisphosphate, a regulator of glycolysis There are two possible answers: it either activates it or inactivates it The simplest approach to the question is just to flip a coin You should stand a 50:50 chance of getting it right The next simplest way is to figure it out Fructose 2,6-bisphosphate stimulates glycolysis by allosterically activating phosphofructo-1-kinase (PFK-1)4 First, decide what should.

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4 It s unfortunate that we have to deal with PFK-1 and PFK-2 PFK-1 is the enzyme that catalyzes the formation of fructose 1,6-bisphospate from fructose 6-phosphate PFK-2 makes the 2,6-bisphosphate

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