answersLogoWhite

0

Synthetase enzymes, also known as ligases, catalyze the joining of two molecules or groups, typically in the presence of ATP or other nucleoside triphosphates, to drive the reaction forward. They play a crucial role in various biochemical pathways, including amino acid activation in protein synthesis and the synthesis of nucleotides and fatty acids. By facilitating the formation of covalent bonds, synthetases are essential for cellular metabolism and the overall functioning of living organisms.

User Avatar

AnswerBot

1mo ago

What else can I help you with?

Continue Learning about Natural Sciences

Where in a cell is argininosuccinate synthetase found?

Agrininosuccinate synthetase is an enzyme that catalyzes the synthesis of argininosuccinate from citrulline and aspartateAs argininosuccinate is in found the urea cycle and the Citrulline-NO cycle the enzyme that produces this is mostly expressed in kidney and liver cells. The gene that codes for the enzyme is found on chromosome 9.


What is The enzyme involved in amino acid activation?

The enzyme involved in amino acid activation is aminoacyl-tRNA synthetase. This enzyme catalyzes the attachment of an amino acid to its corresponding tRNA molecule, a process crucial for protein synthesis. Each aminoacyl-tRNA synthetase is specific to one amino acid and its corresponding tRNA, ensuring the correct amino acid is incorporated into the growing polypeptide chain during translation.


What is the enzyme required to make ATP?

ATP synthtase along with other enzymes and coenzymes .


What is the functional role of a tRNA synthetase enzyme?

It's function is to assemble precursors into product.The transfer Ribo nucleic acid Synthetase has twenty [22 including the alternates] different forms - one tRna synthetase System exists for each amino acid involved.The precursors are the "un-Charged" tRna moiety and its respective amino acid residue.tRna synthetase functions to Charge the 'empty' tRna with [only] the amino acid that is solely associated with It's tRna.This is performed solely by use of the triplet codon system.


How is the enzyme that takes place in the process of amino acids activation for translation called?

The enzyme involved in the activation of amino acids for translation is called aminoacyl-tRNA synthetase. This enzyme catalyzes the attachment of an amino acid to its corresponding tRNA molecule, forming an aminoacyl-tRNA complex. This process is crucial for ensuring that the correct amino acids are incorporated into the growing polypeptide chain during protein synthesis. Each aminoacyl-tRNA synthetase is specific to one amino acid and its corresponding tRNA.

Related Questions

What type of molecule is ATP synthetase?

ATP synthetase is an enzyme that is a type of molecular motor which facilitates the synthesis of ATP from ADP and inorganic phosphate during oxidative phosphorylation in mitochondria.


What is the specific definition of glycogen synthetase?

an enzyme that assists in the breakdown of glycogen


Where in a cell is argininosuccinate synthetase found?

Agrininosuccinate synthetase is an enzyme that catalyzes the synthesis of argininosuccinate from citrulline and aspartateAs argininosuccinate is in found the urea cycle and the Citrulline-NO cycle the enzyme that produces this is mostly expressed in kidney and liver cells. The gene that codes for the enzyme is found on chromosome 9.


What enzyme catalyzes the attachment of an amino acid to tRNA?

Aminoacyl-tRNA synthetase is the enzyme responsible for catalyzing the attachment of an amino acid to tRNA. This process is vital for protein synthesis, ensuring that the correct amino acid is paired with its corresponding tRNA molecule.


What is the role of ATP synthetase in the light dependent reaction?

In the presence of ATP synthetase enzyme ADP is converted in to ATP by uniting one more phosphate bond, storing chemical energy.


What is the enzyme that that charges the RNA molecules with appropriate amino acids?

The enzyme responsible for charging RNA molecules with appropriate amino acids is aminoacyl-tRNA synthetase. It ensures the correct matching of specific amino acids with their corresponding tRNAs during the process of protein synthesis.


What is The enzyme involved in amino acid activation?

The enzyme involved in amino acid activation is aminoacyl-tRNA synthetase. This enzyme catalyzes the attachment of an amino acid to its corresponding tRNA molecule, a process crucial for protein synthesis. Each aminoacyl-tRNA synthetase is specific to one amino acid and its corresponding tRNA, ensuring the correct amino acid is incorporated into the growing polypeptide chain during translation.


What is the major functional difference between succinyl coenzyme A synthetase in plant and animal cell mitochondria?

Succinyl co-enzyme A synthetase in Plants produces ATP while in case Animals It produces GTP (Imran Farooqui) mail me at :- imranfarooqui009@gmail.com


What is the enzyme required to make ATP?

ATP synthtase along with other enzymes and coenzymes .


What is the functional role of a tRNA synthetase enzyme?

It's function is to assemble precursors into product.The transfer Ribo nucleic acid Synthetase has twenty [22 including the alternates] different forms - one tRna synthetase System exists for each amino acid involved.The precursors are the "un-Charged" tRna moiety and its respective amino acid residue.tRna synthetase functions to Charge the 'empty' tRna with [only] the amino acid that is solely associated with It's tRna.This is performed solely by use of the triplet codon system.


How is the enzyme that takes place in the process of amino acids activation for translation called?

The enzyme involved in the activation of amino acids for translation is called aminoacyl-tRNA synthetase. This enzyme catalyzes the attachment of an amino acid to its corresponding tRNA molecule, forming an aminoacyl-tRNA complex. This process is crucial for ensuring that the correct amino acids are incorporated into the growing polypeptide chain during protein synthesis. Each aminoacyl-tRNA synthetase is specific to one amino acid and its corresponding tRNA.


How is glutathione made?

Glutathione is synthesized in the body from three amino acids: cysteine, glutamine, and glycine. The process occurs in two main steps: first, cysteine and glutamate are combined to form gamma-glutamylcysteine, catalyzed by the enzyme gamma-glutamylcysteine synthetase. In the second step, glycine is added to form glutathione, facilitated by the enzyme glutathione synthetase. This tripeptide plays a critical role in antioxidant defense and cellular detoxification.