What type of enzyme is aspartate Transcarbamoylase?

What type of enzyme is aspartate Transcarbamoylase?

Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate (CP) to produce N-carbamoyl-L-aspartate (CAA). This reaction is the first committed step of the pyrimidine biosynthetic pathway.

What is the function of aspartate Transcarbamoylase?

Aspartate transcarbamoylase (ATCase) catalyzes a key step of pyrimidine biosynthesis, the condensation of carbamoyl phosphate with aspartate to form N-carbamoylaspartate. The Escherichia coli enzyme has been extensively studied.

What is the role of zinc in the structure of ATCase?

The catalytic subunit (c) is a 310-residue chain with which enzymatic activity is associated, and a 153-residue regulatory subunit (r) that binds a Zn2+ ion. The role of the regulatory subunits of ATCase is to mediate heterotropic effects, analogous to the Bohr effect or that of 2,3-BPG in hemoglobin.

How is ATCase regulated?

Activity of the ATCase is regulated by shifting the enzyme from a tense, low-affinity state to a relaxed, high-affinity state. ATCase can be seen in the left part of the model in its two states, relaxed (ATCase_R) and tense (ATCase_T).

What is aspartate aminotransferase low?

Low levels of AST are normally found in the blood. When body tissue or an organ such as the heart or liver is diseased or damaged, additional AST is released into the bloodstream. The amount of AST in the blood is directly related to the extent of the tissue damage.

How is a catalyst different from an enzyme?

Catalysts are substances that increase or decrease the rate of a chemical reaction but remain unchanged. Enzymes are proteins that increase rate of chemical reactions converting substrate into product.

How are the allosteric properties of ATCase and hemoglobin similar?

How are the allosteric properties of ATCase and hemoglobin similar? Both are regulated by feedback inhibition. The allostery of both proteins involves regulation by competitive inhibitors. The quaternary structure of both proteins is altered by binding small molecules.

How do ATP and CTP affect the function of ATCase quizlet?

ATP is an activator of ATCase while CTP is an inhibitor. Its activation of ATCase would ensure a balance of purines and pyrimidines. The binding of aspartate to different subunits of ATCase is an example of. A homotropic effect.

How many binding sites are in ATCase?

six active sites
Aspartate carbamoyltransferase (ATCase) is a large dodecameric enzyme with six active sites that exhibits allostery: its catalytic rate is modulated by the binding of various substrates at distal points from the active sites.

What is the R state in ATCase?

In essence, ATCase has two distinct quaternary forms: one that predominates in the absence of substrate or substrate analogs and another that predominates when substrates or analogs are bound. These forms will be referred to as the T (for tense) state and the R (for relaxed) state, respectively.