Acetolactate synthase: Difference between revisions

Latest revision as of 06:04, 16 February 2025

Overview[edit]

Acetolactate synthase (ALS), also known as acetohydroxyacid synthase, is an enzyme that plays a crucial role in the biosynthesis of branched-chain amino acids, such as valine, leucine, and isoleucine. This enzyme catalyzes the first step in the pathway, which involves the condensation of two molecules of pyruvate to form acetolactate.

Function[edit]

Acetolactate synthase is responsible for the conversion of pyruvate into acetolactate, which is a key intermediate in the synthesis of branched-chain amino acids. This reaction is essential for the production of these amino acids, which are vital for protein synthesis and various metabolic processes in plants and microorganisms.

Structure[edit]

ALS is a multi-subunit enzyme that requires the presence of cofactors such as thiamine pyrophosphate (TPP) and flavin adenine dinucleotide (FAD) for its activity. The enzyme is typically composed of large and small subunits, which work together to facilitate the catalytic process.

Inhibition[edit]

Acetolactate synthase is a target for several classes of herbicides, including sulfonylureas and imidazolinones. These herbicides inhibit the enzyme, leading to the disruption of amino acid synthesis and ultimately causing plant death. This makes ALS a critical target for agricultural weed control.

Applications[edit]

The study of acetolactate synthase is important in both agriculture and medicine. In agriculture, understanding ALS can lead to the development of herbicide-resistant crops. In medicine, insights into ALS function can contribute to the development of antibiotics, as the enzyme is present in many pathogenic microorganisms.

Related pages[edit]

@@ Line 1: / Line 1: @@
-{{Short description|Enzyme involved in the biosynthesis of branched-chain amino acids}}
+{{DISPLAYTITLE:Acetolactate Synthase}}
-{{Enzyme}}
-'''Acetolactate synthase''' (ALS), also known as acetohydroxyacid synthase, is an enzyme that catalyzes the first step in the biosynthesis of the branched-chain amino acids [[valine]], [[leucine]], and [[isoleucine]]. This enzyme is found in plants, fungi, and microorganisms, but not in animals, making it a target for herbicides and antibiotics.
+==Overview==
+[[File:Acetolactase_Synthase.png|thumb|right|Diagram of Acetolactate Synthase]]
+'''Acetolactate synthase''' (ALS), also known as acetohydroxyacid synthase, is an enzyme that plays a crucial role in the biosynthesis of branched-chain amino acids, such as [[valine]], [[leucine]], and [[isoleucine]]. This enzyme catalyzes the first step in the pathway, which involves the condensation of two molecules of [[pyruvate]] to form [[acetolactate]].
 ==Function==
-Acetolactate synthase catalyzes the condensation of two molecules of [[pyruvate]] to form [[acetolactate]] in the biosynthesis of valine and leucine. It also catalyzes the condensation of pyruvate and [[2-ketobutyrate]] to form [[acetohydroxybutyrate]] in the biosynthesis of isoleucine. These reactions are the first committed steps in the biosynthetic pathways of these amino acids.
+Acetolactate synthase is responsible for the conversion of pyruvate into acetolactate, which is a key intermediate in the synthesis of branched-chain amino acids. This reaction is essential for the production of these amino acids, which are vital for protein synthesis and various metabolic processes in plants and microorganisms.
 ==Structure==
-ALS is a [[multimeric enzyme]] composed of several subunits. The enzyme requires the cofactor [[thiamine pyrophosphate]] (TPP) and the metal ion [[magnesium]] for its activity. The structure of ALS has been studied extensively to understand its function and to design inhibitors that can serve as herbicides.
+ALS is a multi-subunit enzyme that requires the presence of cofactors such as [[thiamine pyrophosphate]] (TPP) and [[flavin adenine dinucleotide]] (FAD) for its activity. The enzyme is typically composed of large and small subunits, which work together to facilitate the catalytic process.
 ==Inhibition==
-Acetolactate synthase is the target of several classes of herbicides, including the [[sulfonylureas]], [[imidazolinones]], and [[triazolopyrimidines]]. These herbicides inhibit ALS by binding to the enzyme and preventing it from catalyzing its reactions. The inhibition of ALS leads to the depletion of branched-chain amino acids, which is lethal to plants.
+Acetolactate synthase is a target for several classes of herbicides, including sulfonylureas and imidazolinones. These herbicides inhibit the enzyme, leading to the disruption of amino acid synthesis and ultimately causing plant death. This makes ALS a critical target for agricultural weed control.
-==Clinical significance==
+==Applications==
-While ALS is not present in animals, its inhibition is important in agriculture for controlling weed growth. The development of ALS-inhibiting herbicides has been a major advancement in crop protection. However, the widespread use of these herbicides has led to the evolution of herbicide-resistant weed species.
+The study of acetolactate synthase is important in both agriculture and medicine. In agriculture, understanding ALS can lead to the development of herbicide-resistant crops. In medicine, insights into ALS function can contribute to the development of antibiotics, as the enzyme is present in many pathogenic microorganisms.
-==Biotechnological applications==
-ALS is used in [[metabolic engineering]] to produce branched-chain amino acids in microorganisms. By manipulating the expression of ALS and other enzymes in the pathway, it is possible to increase the yield of these amino acids for industrial purposes.
 ==Related pages==
 * [[Branched-chain amino acid]]
-* [[Herbicide resistance]]
 * [[Enzyme inhibition]]
-* [[Metabolic engineering]]
+* [[Herbicide]]
+* [[Pyruvate]]
-==Gallery==
-<gallery>
-File:Acetolactase_Synthase.png|Structure of acetolactate synthase
-</gallery>
 [[Category:Enzymes]]
-[[Category:Amino acid biosynthesis]]
+[[Category:Amino acid metabolism]]
-[[Category:Herbicides]]