UDP-N-acetylmuramate—L-alanine Ligase
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UDP-N-acetylmuramate—L-alanine Ligase
In enzymology, a UDP-''N''-acetylmuramate—L-alanine ligase () is an enzyme that catalyzes the chemical reaction :ATP + UDP-N-acetylmuramate + L-alanine \rightleftharpoons ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine The 3 substrates of this enzyme are ATP, UDP-N-acetylmuramate, and L-alanine, whereas its 3 products are ADP, phosphate, and UDP-N-acetylmuramoyl-L-alanine. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is UDP-N-acetylmuramate:L-alanine ligase (ADP-forming). Other names in common use include MurC synthetase, UDP-N-acetylmuramoyl-L-alanine synthetase, uridine diphospho-N-acetylmuramoylalanine synthetase, UDP-N-acetylmuramoylalanine synthetase, L-alanine-adding enzyme, UDP-acetylmuramyl-L-alanine synthetase, UDPMurNAc-L-alanine synthetase, L-Ala ligase, uridine diphosphate N-acetylmuramate:L-alanine ligase, uridine 5'-di ...
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Enzymology
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Muramyl Ligase
The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages: # formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc). # addition of a short polypeptide chain to the UDPMurNAc. # addition of a second GlcNAc to the disaccharide- pentapeptide building block and transport of this unit through the cytoplasmic membrane and incorporation into the growing peptidoglycan layer. Stage two involves four key Mur ligase enzymes: MurC, MurD, MurEEC and MurFEC. These four Mur ligases are responsible for the successive additio ...
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Protein Data Bank
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules such as proteins and nucleic acids, which is overseen by the Worldwide Protein Data Bank (wwPDB). This structural data is obtained and deposited by biologists and biochemists worldwide through the use of experimental methodologies such as X-ray crystallography, Nuclear magnetic resonance spectroscopy of proteins, NMR spectroscopy, and, increasingly, cryo-electron microscopy. All submitted data are reviewed by expert Biocuration, biocurators and, once approved, are made freely available on the Internet under the CC0 Public Domain Dedication. Global access to the data is provided by the websites of the wwPDB member organizations (PDBe, PDBj, RCSB PDB, and BMRB). The PDB is a key in areas of structural biology, such as structural genomics. Most major scientific journals and some funding agencies now require scientists to submit their structure data to the PDB. Many other ...
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Tertiary Structure
Protein tertiary structure is the three-dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates. These coordinates may refer either to a protein domain or to the entire tertiary structure. A number of these structures may bind to each other, forming a quaternary structure. History The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demon ...
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Peptidoglycan Biosynthesis
Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like layer (sacculus) that surrounds the bacterial cytoplasmic membrane. The sugar component consists of alternating residues of β-(1,4) linked ''N''-acetylglucosamine (NAG) and ''N''-acetylmuramic acid (NAM). Attached to the ''N''-acetylmuramic acid is an oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by peptidoglycan production. Peptidoglycan hydrolysis and synthesis are two processes that must occur in ord ...
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List Of Enzymes
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: :Oxidoreductases (EC 1) ( Oxidoreductase) * Dehydrogenase * Luciferase * DMSO reductase :EC 1.1 (act on the CH-OH group of donors) * :EC 1.1.1 (with NAD+ or NADP+ as acceptor) ** Alcohol dehydrogenase (NAD) ** Alcohol dehydrogenase (NADP) ** Homoserine dehydrogenase ** Aminopropanol oxidoreductase ** Diacetyl reductase ** Glycerol dehydrogenase ** Propanediol-phosphate dehydrogenase ** glycerol-3-phoshitiendopene dehydrogenase (NAD+) ** D-xylulose reductase ** L-xylulose reductase ** Lactate dehydrogenase ** Malate dehydrogenase ** Isocitrate dehydrogenase ** HMG-CoA reductase * :EC 1.1.2 (with a cytochrome as acceptor) * :EC 1.1.3 (with oxygen as acceptor) ** Glucose oxidase ** L-gulonolactone oxidase ** Thiamine oxidase ** Xanthine oxidase * EC 1.1.4 (with a disulfide as accep ...
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Ligase
In biochemistry, a ligase is an enzyme that can catalyze the joining ( ligation) of two molecules by forming a new chemical bond. This is typically via hydrolysis of a small pendant chemical group on one of the molecules, typically resulting in the formation of new C-O, C-S, or C-N bonds. For example, DNA ligase can join two complementary fragments of nucleic acid by forming phosphodiester bonds, and repair single stranded breaks that arise in double stranded DNA during replication. In general, a ligase catalyzes the following dehydration reaction, thus joining molecules A and B: A-OH + B-H → A–B + H2O Nomenclature The naming of ligases is inconsistent and so these enzymes are commonly known by several different names. Generally, the common names of ligases include the word "ligase", such as in DNA ligase, an enzyme commonly used in molecular biology laboratories to join together DNA fragments. However, many common names use the term "synthetase" or "synthase" instead, ...
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Phosphate
Phosphates are the naturally occurring form of the element phosphorus. In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid, phosphoric acid . The phosphate or orthophosphate ion is derived from phosphoric acid by the removal of three protons . Removal of one proton gives the dihydrogen phosphate ion while removal of two protons gives the hydrogen phosphate ion . These names are also used for salts of those anions, such as ammonium dihydrogen phosphate and trisodium phosphate. File:3-phosphoric-acid-3D-balls.png, Phosphoricacid File:2-dihydrogenphosphate-3D-balls.png, Dihydrogenphosphate File:1-hydrogenphosphate-3D-balls.png, Hydrogenphosphate File:0-phosphate-3D-balls.png, Phosphate or orthophosphate In organic chemistry, phosphate or orthophosphate is an organophosphate, an ester of orthophosphoric acid of the form where one ...
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Enzyme
An enzyme () is a protein that acts as a biological catalyst by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts include Ribozyme, catalytic RNA molecules, also called ribozymes. They are sometimes descr ...
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Adenosine Diphosphate
Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells. ADP consists of three important structural components: a sugar backbone attached to adenine and two phosphate groups bonded to the 5 carbon atom of ribose. The diphosphate group of ADP is attached to the 5’ carbon of the sugar backbone, while the adenine attaches to the 1’ carbon. ADP can be interconverted to adenosine triphosphate (ATP) and adenosine monophosphate (AMP). ATP contains one more phosphate group than ADP, while AMP contains one fewer phosphate group. Energy transfer used by all living things is a result of dephosphorylation of ATP by enzymes known as ATPases. The cleavage of a phosphate group from ATP results in the coupling of energy to metabolic reactions and a by-product of ADP. ATP is continually reformed from lower-energy species ADP and AMP. The biosynthesis of ATP is achieved th ...
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