Environmental
Rachman proposed three pathways for the development of phobias: direct or classical conditioning (exposure to phobic stimulus), vicarious acquisition (seeing others experience phobic stimulus), and informational/instructional acquisition (learning about phobic stimulus from others). Classical conditioning
Much of the progress in understanding the acquisition of fear responses in phobias can be attributed to classical conditioning (Pavlovian model). When an aversive stimulus and a neutral one are paired together, for instance, when an electric shock is given in a specific room, the subject can start to fear not only the shock but the room as well. In behavioral terms, the room is a conditioned stimulus (CS). When paired with an aversive unconditioned stimulus (UCS) (the shock), it creates a conditioned response (CR) (fear for the room) (CS+UCS=CR). For example, in case of the fear of heights (acrophobia), the CS is heights. Such as a balcony on the top floors of a high rise building. The UCS can originate from an aversive or traumatizing event in the persons life, such as almost falling from a great height. The original fear of nearly falling is associated with being high, leading to a fear of heights. In other words, the CS (heights) associated with the aversive UCS (almost falling) leads to the CR (fear). Though historically influential in the theory of fear acquisition, this direct conditioning model is not the only proposed way to acquire a phobia. This theory in fact has limitations as not everyone that has experienced a traumatic event develops a phobia and vice versa.
These and other novel genes (dptI, dptJ) are believed to be involved in supplying the nonproteinogenic amino acids L-3-methylglutamic acid and Kyn; they are located next to the NRPS genes.The decanoic acid portion of daptomycin is synthesized by fatty acid synthase machinery (Figure 2). Post-translational modification of the apo-acyl carrier protein (ACP, thiolation, or T domain) by a phosphopantetheinyltransferase (PPTase) enzyme catalyzes the transfer of a flexible phosphopantetheine arm from coenzyme A to a conserved serine in the ACP domain through a phosphodiester linkage. The holo-ACP can provide a thiol on which the substrate and acyl chains are covalently bound during chain elongations. The two core catalytic domains are an acyltransferase (AT) and a ketosynthase (KS). The AT acts upon a malonyl-CoA substrate and transfers an acyl group to the thiol of the ACP domain. This net transthiolation is an energy-neutral step. Next, the acyl-S-ACP gets transthiolated to a conserved cysteine on the KS; the KS decarboxylates the downstream malonyl-S-ACP and forms a β-ketoacyl-S-ACP. This serves as the substrate for the next cycle of elongation. Before the next cycle begins, however, the β-keto group undergoes reduction to the corresponding alcohol catalyzed by a ketoreductase domain, followed by dehydration to the olefin catalyzed by a dehydratase domain, and finally reduction to the methylene catalyzed by an enoylreductase domain. Each KS catalytic cycle results in the net addition of two carbons.