Bioorganic Chemistry: A Chemical Approach to Enzyme Action by Hermann Dugas

By Hermann Dugas

New textbooks in any respect degrees of chemistry seem with nice regularity. So me fields equivalent to uncomplicated biochemistry, natural response mechanisms, weIl represented through many glorious and chemical thermodynamics are texts, and new or revised versions are released sufficiently usually to maintain with development in study. notwithstanding, a few parts of chemistry, specifically a lot of these taught on the graduate point, be afflicted by areal loss of up to date textbooks. the main critical wishes happen in fields which are swiftly altering. Textbooks in those topics frequently must be written via scientists really occupied with the examine that's advancing the sector. it's not usually effortless to cajole such contributors to set time apart to assist unfold the data they've got accrued. Our target, during this sequence, is to pinpoint components of chemistry the place contemporary growth has outpaced what's lined in any to be had textbooks, after which hunt down and consistent with suade specialists in those fields to provide particularly concise yet instructive introductions to their fields. those should still serve the wishes of 1 semester or one sector graduate classes in chemistry and biochem­ istry. often times the supply of texts in energetic study components can assist stimulate the production of recent classes. Charles R. Cantor vii Preface to the 3rd variation It used to be over a hundred years in the past that Emil Fischer postulated his inventive "lock-and-key" precept, whieh used to be in this case utilized to the devel­ opment of a latest concept of enzyme catalysis.

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This, very likely, results from a conformational change on the ribosome which again requires energy at the expense of a molecule of GTP. The aminoacyl site is now empty, and the mRNA has also shifted (translocation), so that it can now dictate the entrance of a new aminoacyl-tRNA to the aminoacyl site. Once this has occurred, peptide bond formation (to give a tripeptide) can take place, thus repeating the sequence of events as described (Fig. 1). This provides a basic description of in vivo protein synthesis, neglecting details such as the involvement of pro tein elongation factors.

The first is to convert the amino-protected amino acid to an activated form and then react this with the amino function of a second amino acid. As will be recalled, activation is necessary since work must be done during peptide bond formation. Alternatively, it is possible to react two amino acids together (one amino protected, the other carboxyl protected) in the presence of a coupling agent that activates the carboxyl function in situ. In the synthesis of a protein macromolecule, peptide bond formation must be a high-yield reaction.

The stage is now set for the synthesis of the peptide linkage. The second amino acid (aminoacyl-tRNA) also binds on the ribosome (at the so-called aminoacyl site) in close proximity to the fMet-tRNA fMet . While no chemical reaction has yet occurred, this binding process requires work, the energy of which comes from a molecule of GTP (guanosine triphosphate; like ATP except adenine is replaced with guanine). The amino function of the aminoacyl-tRNA now attacks the f-methionine, at which point the tRNA fMet becomes a leaving groUP, and the peptide bond is formed.

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