Does Peptide Bond Formation Require GTP?

by | Last updated on January 24, 2024

, , , ,

14a); Hydrolysis of GTP by EF-Tu/Ts is not required for binding aminoacyl tRNA to the ribosome, but

is required for peptide bond formation

(T18. … 16); The ternary complex would only form with charged tRNAs destined for binding to the A site (F18.

Does peptidyl transferase require energy?

Function. Peptidyl transferase

speeds up the reaction by lowering its energy of activation

. It does this by providing proper orientation for the reaction to occur.

Does peptidyl transferase require GTP?

∑ EF-Tu and EF-Ts are required for binding aminoacyl-tRNAs to the ribosome;

EF-Tu/Ts requires GTP to bind to the ribosome

(F18.

What activates peptidyl transferase?

The substrates for the peptidyl transferase reaction are

two tRNA molecules

, one bearing the growing peptide chain and the other bearing the amino acid that will be added to the chain.

Does tRNA synthetase use GTP?

Since the A site must be open for binding of the next aminoacyl-tRNA, the peptidyl-tRNA must be moved over to the P site.

The elongation factor EF-G uses one GTP to catalyze

this process, and both the mRNA and peptidyl-tRNA move the distance of one codon. The deacylated tRNA moves to the E site.

Which drug inhibits peptidyl transferase?

The first broad-spectrum antibiotic

chloramphenicol

and one of the newest clinically important antibacterials, linezolid, inhibit protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome.

Which step of translation requires the most energy?


Making Aminoacyl-tRNAs

.

Translation

is perhaps the most energy-intensive job a cell must do, beginning with the attachment of amino acids to their tRNAs. The basic amino-acylation reaction is the same for all amino acids. A specific aminoacyl-tRNA synthase attaches each tRNA to (charges) an appropriate amino acid.

What catalyzes peptidyl transferase reaction?


The ribosome

catalyzes two fundamental biological reactions: peptidyl transfer, the formation of a peptide bond during protein synthesis, and peptidyl hydrolysis, the release of the complete protein from the peptidyl tRNA upon completion of translation.

What occurs translation?

Translation occurs in a structure called the ribosome, which is a

factory for the synthesis of proteins

What is the peptidyl transferase center?

The ribosomal peptidyl transferase center (PTC)

resides in the large ribosomal subunit

and catalyzes the two principal chemical reactions of protein synthesis: peptide bond formation and peptide release. … The crystallographic structures compellingly confirmed that peptidyl transferase is an RNA enzyme.

What is required for protein synthesis?

Section 29.1Protein Synthesis Requires

the Translation of Nucleotide Sequences Into Amino Acid Sequences

. … A protein is synthesized in the amino-to-carboxyl direction by the sequential addition of amino acids to the carboxyl end of the growing peptide chain (Figure 29.2).

Is tRNA a ribosome?

A ribosome is a molecular machine that synthesizes proteins in the cell. It consists of two main parts, a large and small subunit. The ribosome brings together the mRNA to be translated and a set of molecules called transfer RNAs, or tRNAs, which are floating in the cell.

What is the charging of tRNA?

Amino acid activation (also known as aminoacylation or tRNA charging) refers

to the attachment of an amino acid to its Transfer RNA (tRNA)

. Aminoacyl transferase binds Adenosine triphosphate (ATP) to amino acid, PP is released. Aminoacyl TRNA synthetase binds AMP-amino acid to tRNA. The AMP is used in this step.

Which amino acid is most basic?


Histidine

is an alpha-amino acid with an imidazole functional group. So as it contains the most basic nitrogen atom, it is the most basic amino acid.

Which of the following prokaryotic rRNA has the peptidyl transferase activity?

The enzymatic activity of the ribosome is called peptidyl transferase and in bacteria is conferred on the 50S subunit by

the 23S rRNA

, which is why the ribosome is a type of ribozyme.

How is GTP used during elongation?

During elongation, GTP

facilitates the binding of a new aminoacyl tRNA to the A site of a ribosome

. GTP is also an important factor in signal transduction pathways. Here, GTP can be associated with G-protein complexes and is used to regulate the activity of the protein.

Charlene Dyck
Author
Charlene Dyck
Charlene is a software developer and technology expert with a degree in computer science. She has worked for major tech companies and has a keen understanding of how computers and electronics work. Sarah is also an advocate for digital privacy and security.