Enzymes that catalyze the joining of either ammonia or an amide with another molecule, in which the linkage is in the form of a carbon-nitrogen bond. EC 6.3.1.
Organic compounds containing the -CO-NH2 radical. Amides are derived from acids by replacement of -OH by -NH2 or from ammonia by the replacement of H by an acyl group. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Large enzyme complexes composed of a number of component enzymes that are found in STREPTOMYCES which biosynthesize MACROLIDES and other polyketides.
A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.
An enzyme that converts UDP glucosamine into chitin and UDP. EC 2.4.1.16.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Amidohydrolases are enzymes that catalyze the hydrolysis of amides and related compounds, playing a crucial role in various biological processes including the breakdown and synthesis of bioactive molecules.

Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. (1/66)

The gene thiI encodes a protein (ThiI) that plays a role in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine, but the reaction catalyzed by ThiI remains undetermined. Based upon sequence alignments, ThiI shares a unique "P-loop" motif with the PPi synthetase family, four enzymes that catalyze adenylation and subsequent substitution of carbonyl oxygens. To test whether or not this motif is critical for ThiI function, the Asp in the motif was converted to Ala (D189A), and a screen for in vivo 4-thiouridine production revealed the altered enzyme to be inactive. Further scrutiny of sequence data and the crystal structures of two members of the PPi synthetase family implicated Lys321 in the proposed adenylation function of ThiI, and the critical nature of Lys321 has been demonstrated by site-directed mutagenesis and genetic screening. Our results, then, indicate that ThiI catalyzes the adenylation of a substrate at the expense of ATP, a narrowing of possible reactions that provides a strong new basis for deducing the early steps in the transfer of sulfur from cysteine to both thiamin and 4-thiouridine.  (+info)

Identification of the novobiocin biosynthetic gene cluster of Streptomyces spheroides NCIB 11891. (2/66)

The novobiocin biosynthetic gene cluster from Streptomyces spheroides NCIB 11891 was cloned by using homologous deoxynucleoside diphosphate (dNDP)-glucose 4,6-dehydratase gene fragments as probes. Double-stranded sequencing of 25.6 kb revealed the presence of 23 putative open reading frames (ORFs), including the gene for novobiocin resistance, gyrB(r), and at least 11 further ORFs to which a possible role in novobiocin biosynthesis could be assigned. An insertional inactivation experiment with a dNDP-glucose 4, 6-dehydratase fragment resulted in abolishment of novobiocin production, since biosynthesis of the deoxysugar moiety of novobiocin was blocked. Heterologous expression of a key enzyme of novobiocin biosynthesis, i.e., novobiocic acid synthetase, in Streptomyces lividans TK24 further confirmed the involvement of the analyzed genes in the biosynthesis of the antibiotic.  (+info)

Cloning, overexpression, and purification of novobiocic acid synthetase from Streptomyces spheroides NCIMB 11891. (3/66)

Novobiocic acid synthetase, a key enzyme in the biosynthesis of the antibiotic novobiocin, was cloned from the novobiocin producer Streptomyces spheroides NCIMB 11891. The enzyme is encoded by the gene novL, which codes for a protein of 527 amino acids with a calculated mass of 56,885 Da. The protein was overexpressed as a His(6) fusion protein in Escherichia coli and purified to apparent homogeneity by affinity chromatography and gel chromatography. The purified enzyme catalyzed the formation of an amide bond between 3-dimethylallyl-4-hydroxybenzoic acid (ring A of novobiocin) and 3-amino-4,7-dihydroxy-8-methyl coumarin (ring B of novobiocin) in an ATP-dependent reaction. NovL shows homology to the superfamily of adenylate-forming enzymes, and indeed the formation of an acyl adenylate from ring A and ATP was demonstrated by an ATP-PP(i) exchange assay. The purified enzyme exhibited both activation and transferase activity, i.e. it catalyzed both the activation of ring A as acyl adenylate and the subsequent transfer of the acyl group to the amino group of ring B. It is active as a monomer as determined by gel filtration chromatography. The reaction was specific for ATP as nucleotide triphosphate and dependent on the presence of Mg(2+) or Mn(2+). Apparent K(m) values for ring A and ring B were determined as 19 and 131 micrometer respectively. Of several analogues of ring A, only 3-geranyl-4-hydroxybenzoate and to a lesser extent 3-methyl-4-aminobenzoate were accepted as substrates.  (+info)

Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. (4/66)

Trypanothione [N1,N8-bis(glutathionyl)spermidine] is a unique metabolite found only in trypanosomatids, where it subsumes many of the functions of GSH in other organisms. In Crithidia fasciculata, two distinct ATP-dependent ligases, glutathionylspermidine synthetase (GspS; EC 6.3.1.8) and trypanothione synthetase (TryS; EC 6.3.1.9), are involved in the synthesis of trypanothione from GSH and spermidine. Both enzymes have been cloned previously, but expression in Escherichia coli produced insoluble and inactive protein. Here we report on the successful expression of soluble (His)6-tagged C. fasciculata GspS in E. coli. Following purification using nickel-chelating affinity chromatography, the tag sequence was removed and the enzyme purified to homogeneity by anion-exchange chromatography. The kinetic parameters of the recombinant enzyme have been determined using a coupled enzyme assay and also by HPLC analysis of end-product formation. Under optimal conditions (0.1 M K+-Hepes, pH 7.3) GspS has synthetase activity with apparent K(m) values for GSH, spermidine and MgATP of 242, 59 and 114 microM respectively, and a k(cat) of 15.5 s(-1). Glutathionylspermidine is formed as end product and the enzyme lacks TryS activity. Like E. coli GspS, the recombinant enzyme also possesses amidase activity (EC 3.5.1.78), hydrolysing glutathionylspermidine to GSH and spermidine with a k(cat) of 0.38 s(-1) and a K(m) of 500 microM. GspS can also hydrolyse trypanothione at about 1.5% of the rate with glutathionylspermidine. A single amino acid mutation (Cys-79-->Ala) is shown to ablate the amidase activity without affecting the synthetase activity.  (+info)

A single enzyme catalyses formation of Trypanothione from glutathione and spermidine in Trypanosoma cruzi. (5/66)

Protozoa of the order Kinetoplastida differ from other organisms in their ability to conjugate glutathione (l-gamma-glutamyl-cysteinyl-glycine) and spermidine to form trypanothione [N(1),N(8)-bis(glutathionyl)spermidine], a metabolite involved in defense against chemical and oxidant stress and other biosynthetic functions. In Crithidia fasciculata, trypanothione is synthesized from GSH and spermidine via the intermediate glutathionylspermidine in two distinct ATP-dependent reactions catalyzed by glutathionylspermidine synthetase (GspS; EC ) and trypanothione synthetase (TryS; EC ), respectively. Here we have cloned a single copy gene (TcTryS) from Trypanosoma cruzi encoding a protein with 61% sequence identity with CfTryS but only 31% with CfGspS. Saccharomyces cerevisiae transformed with TcTryS were able to synthesize glutathionylspermidine and trypanothione, suggesting that this enzyme is able to catalyze both biosynthetic steps, unlike CfTryS. When cultures were supplemented with aminopropylcadaverine, yeast transformants contained glutathionylaminopropylcadaverine and homotrypanothione [N(1),N(9)-bis(glutathionyl)aminopropylcadaverine], metabolites that have been previously identified in T. cruzi, but not in C. fasciculata. Kinetic studies on recombinant TcTryS purified from Escherichia coli revealed that the enzyme displays high-substrate inhibition with glutathione (K(m) and K(i) of 0.57 and 1.2 mm, respectively, and k(cat) of 3.4 s(-1)), but obeys Michaelis-Menten kinetics with spermidine, aminopropylcadaverine, glutathionylspermidine, and MgATP as variable substrate. The recombinant enzyme possesses weak amidase activity and can hydrolyze trypanothione, homotrypanothione, or glutathionylspermidine to glutathione and the corresponding polyamine.  (+info)

Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications. (6/66)

Bacillus stearothermophilus H-804 isolated from a hot spring in Beppu, Japan, produced an ammonia-specific NAD synthetase (EC 6.3.1.5). The enzyme specifically used NH3 as an amide donor for the synthesis of NAD as it formed AMP and pyrophosphate from deamide-NAD and ATP. None of the l-amino acids tested, such as l-asparagine or l-glutamine, or other amino compounds such as urea, uric acid, or creatinine was used instead of NH3. Mg2+ was needed for the activity, and the maximum enzyme activity was obtained with 3 mM MgCl2. The molecular mass of the native enzyme was 50 kDa by gel filtration, and SDS-PAGE showed a single protein band at the molecular mass of 25 kDa. The optimum pH and temperature for the activity were from 9.0 to 10.0 and 60 degrees C, respectively. The enzyme was stable at a pH range of 7.5 to 9.0 and up to 60 degrees C. The Km for NH3, ATP, and deamide-NAD were 0.91, 0.052, and 0.028 mM, respectively. The gene encoding the enzyme consisted of an open reading frame of 738 bp and encoded a protein of 246 amino acid residues. The deduced amino acid sequence of the gene had about 32% homology to those of Escherichia coli and Bacillus subtilis NAD synthetases. We caused the NAD synthetase gene to be expressed in E. coli at a high level; the enzyme activity (per liter of medium) produced by the recombinant E. coli was 180-fold that of B. stearothermophilus H-804. The specific assay of ammonia and ATP (up to 25 microM) with this stable NAD synthetase was possible.  (+info)

Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. (7/66)

NAD synthetase catalyzes the final step in the biosynthesis of NAD. In the present study, we obtained cDNAs for two types of human NAD synthetase (referred as NADsyn1 and NADsyn2). Structural analysis revealed in both NADsyn1 and NADsyn2 a domain required for NAD synthesis from ammonia and in only NADsyn1 an additional carbon-nitrogen hydrolase domain shared with enzymes of the nitrilase family that cleave nitriles as well as amides to produce the corresponding acids and ammonia. Consistent with the domain structures, biochemical assays indicated (i) that both NADsyn1 and NADsyn2 have NAD synthetase activity, (ii) that NADsyn1 uses glutamine as well as ammonia as an amide donor, whereas NADsyn2 catalyzes only ammonia-dependent NAD synthesis, and (iii) that mutant NADsyn1 in which Cys-175 corresponding to the catalytic cysteine residue in nitrilases was replaced with Ser does not use glutamine. Kinetic studies suggested that glutamine and ammonia serve as physiological amide donors for NADsyn1 and NADsyn2, respectively. Both synthetases exerted catalytic activity in a multimeric form. In the mouse, NADsyn1 was seen to be abundantly expressed in the small intestine, liver, kidney, and testis but very weakly in the skeletal muscle and heart. In contrast, expression of NADsyn2 was observed in all tissues tested. Therefore, we conclude that humans have two types of NAD synthetase exhibiting different amide donor specificity and tissue distributions. The ammonia-dependent synthetase has not been found in eucaryotes until this study. Our results also indicate that the carbon-nitrogen hydrolase domain is the functional domain of NAD synthetase to make use of glutamine as an amide donor in NAD synthesis. Thus, glutamine-dependent NAD synthetase may be classified as a possible glutamine amidase in the nitrilase family. Our molecular identification of NAD synthetases may prove useful to learn more of mechanisms regulating cellular NAD metabolism.  (+info)

Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase. (8/66)

NAD+ is an essential co-enzyme for redox reactions and is consumed in lysine deacetylation and poly(ADP-ribosyl)ation. NAD+ synthetase catalyzes the final step in NAD+ synthesis in the well characterized de novo, salvage, and import pathways. It has been long known that eukaryotic NAD+ synthetases use glutamine to amidate nicotinic acid adenine dinucleotide while many purified prokaryotic NAD+ synthetases are ammonia-dependent. Earlier, we discovered that glutamine-dependent NAD+ synthetases contain N-terminal domains that are members of the nitrilase superfamily and hypothesized that these domains function as glutamine amidotransferases for the associated synthetases. Here we show yeast glutamine-dependent NAD+ synthetase Qns1 requires both the nitrilase-related active-site residues and the NAD+ synthetase active-site residues for function in vivo. Despite failure to complement the lethal phenotype of qns1 disruption, the former mutants retain ammonia-dependent NAD+ synthetase activity in vitro, whereas the latter mutants retain basal glutaminase activity. Moreover, the two classes of mutants fail to trans-complement despite forming a stable heteromultimer in vivo. These data indicate that the nitrilase-related domain in Qns1 is the fourth independently evolved glutamine amidotransferase domain to have been identified in nature and that glutamine-dependence is an obligate phenomenon involving intramolecular transfer of ammonia over a predicted distance of 46 A from one active site to another within Qns1 monomers.  (+info)

Amide synthases are a class of enzymes that catalyze the formation of amide bonds between two molecules. Specifically, they facilitate the reaction between a carboxylic acid and an amine to produce an amide. This process is also known as amide bond formation or amide synthesis.

In the context of medical research and therapeutic development, amide synthases are important for understanding the biosynthesis of various endogenous compounds, such as peptides and proteins, as well as for developing methods to synthesize novel drugs and pharmaceutical agents.

There are several types of amide synthases, including:

1. Non-ribosomal peptide synthetases (NRPS): These enzymes catalyze the formation of complex peptides without the involvement of ribosomes. They typically consist of multiple modules, each of which is responsible for adding a single amino acid to the growing peptide chain.
2. Amidotransferases: These enzymes transfer an amino group from a donor molecule (usually glutamine) to a carboxylic acid, resulting in the formation of an amide bond. They are involved in various metabolic pathways, including the biosynthesis of amino acids, nucleotides, and other biomolecules.
3. Amide synthetases involved in lipid metabolism: These enzymes catalyze the formation of amide bonds between fatty acids and various amine-containing molecules, such as sphingosine or serine, during the biosynthesis of complex lipids like sphingolipids and glycerophospholipids.

Understanding the function and regulation of amide synthases is crucial for developing strategies to modulate their activity in various disease contexts, including infectious diseases, cancer, and neurodegenerative disorders.

An amide is a functional group or a compound that contains a carbonyl group (a double-bonded carbon atom) and a nitrogen atom. The nitrogen atom is connected to the carbonyl carbon atom by a single bond, and it also has a lone pair of electrons. Amides are commonly found in proteins and peptides, where they form amide bonds (also known as peptide bonds) between individual amino acids.

The general structure of an amide is R-CO-NHR', where R and R' can be alkyl or aryl groups. Amides can be classified into several types based on the nature of R and R' substituents:

* Primary amides: R-CO-NH2
* Secondary amides: R-CO-NHR'
* Tertiary amides: R-CO-NR''R'''

Amides have several important chemical properties. They are generally stable and resistant to hydrolysis under neutral or basic conditions, but they can be hydrolyzed under acidic conditions or with strong bases. Amides also exhibit a characteristic infrared absorption band around 1650 cm-1 due to the carbonyl stretching vibration.

In addition to their prevalence in proteins and peptides, amides are also found in many natural and synthetic compounds, including pharmaceuticals, dyes, and polymers. They have a wide range of applications in chemistry, biology, and materials science.

Polyketide synthases (PKSs) are a type of large, multifunctional enzymes found in bacteria, fungi, and other organisms. They play a crucial role in the biosynthesis of polyketides, which are a diverse group of natural products with various biological activities, including antibiotic, antifungal, anticancer, and immunosuppressant properties.

PKSs are responsible for the assembly of polyketide chains by repetitively adding two-carbon units derived from acetyl-CoA or other extender units to a growing chain. The PKS enzymes can be classified into three types based on their domain organization and mechanism of action: type I, type II, and type III PKSs.

Type I PKSs are large, modular enzymes that contain multiple domains responsible for different steps in the polyketide biosynthesis process. These include acyltransferase (AT) domains that load extender units onto the PKS, acyl carrier proteins (ACPs) that tether the growing chain to the PKS, and ketosynthase (KS) domains that catalyze the condensation of the extender unit with the growing chain.

Type II PKSs are simpler enzymes that consist of several separate proteins that work together in a complex to synthesize polyketides. These include ketosynthase, acyltransferase, and acyl carrier protein domains, as well as other domains responsible for reducing or modifying the polyketide chain.

Type III PKSs are the simplest of the three types and consist of a single catalytic domain that is responsible for both loading extender units and catalyzing their condensation with the growing chain. These enzymes typically synthesize shorter polyketide chains, such as those found in certain plant hormones and pigments.

Overall, PKSs are important enzymes involved in the biosynthesis of a wide range of natural products with significant medical and industrial applications.

Alkyl and aryl transferases are a group of enzymes that catalyze the transfer of alkyl or aryl groups from one molecule to another. These enzymes play a role in various biological processes, including the metabolism of drugs and other xenobiotics, as well as the biosynthesis of certain natural compounds.

Alkyl transferases typically catalyze the transfer of methyl or ethyl groups, while aryl transferases transfer larger aromatic rings. These enzymes often use cofactors such as S-adenosylmethionine (SAM) or acetyl-CoA to donate the alkyl or aryl group to a recipient molecule.

Examples of alkyl and aryl transferases include:

1. Methyltransferases: enzymes that transfer methyl groups from SAM to various acceptor molecules, such as DNA, RNA, proteins, and small molecules.
2. Histone methyltransferases: enzymes that methylate specific residues on histone proteins, which can affect chromatin structure and gene expression.
3. N-acyltransferases: enzymes that transfer acetyl or other acyl groups to amino groups in proteins or small molecules.
4. O-acyltransferases: enzymes that transfer acyl groups to hydroxyl groups in lipids, steroids, and other molecules.
5. Arylsulfatases: enzymes that remove sulfate groups from aromatic rings, releasing an alcohol and sulfate.
6. Glutathione S-transferases (GSTs): enzymes that transfer the tripeptide glutathione to electrophilic centers in xenobiotics and endogenous compounds, facilitating their detoxification and excretion.

Chitin synthase is an enzyme that is responsible for the biosynthesis of chitin, which is a long-chain polymer of N-acetylglucosamine. Chitin is a structural component in the exoskeletons of arthropods, such as insects and crustaceans, as well as in the cell walls of fungi.

Chitin synthase catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to a growing chitin chain. There are several different isoforms of chitin synthase, which are classified based on their sequence similarity and biochemical properties. These isoforms play distinct roles in the biosynthesis of chitin in different organisms.

Inhibitors of chitin synthase have been developed as potential therapeutic agents for the control of insect pests and fungal pathogens.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Amidohydrolases are a class of enzymes that catalyze the hydrolysis of amides and related compounds, resulting in the formation of an acid and an alcohol. This reaction is also known as amide hydrolysis or amide bond cleavage. Amidohydrolases play important roles in various biological processes, including the metabolism of xenobiotics (foreign substances) and endogenous compounds (those naturally produced within an organism).

The term "amidohydrolase" is a broad one that encompasses several specific types of enzymes, such as proteases, esterases, lipases, and nitrilases. These enzymes have different substrate specificities and catalytic mechanisms but share the common ability to hydrolyze amide bonds.

Proteases, for example, are a major group of amidohydrolases that specifically cleave peptide bonds in proteins. They are involved in various physiological processes, such as protein degradation, digestion, and regulation of biological pathways. Esterases and lipases hydrolyze ester bonds in various substrates, including lipids and other organic compounds. Nitrilases convert nitriles into carboxylic acids and ammonia by cleaving the nitrile bond (C≡N) through hydrolysis.

Amidohydrolases are found in various organisms, from bacteria to humans, and have diverse applications in industry, agriculture, and medicine. For instance, they can be used for the production of pharmaceuticals, biofuels, detergents, and other chemicals. Additionally, inhibitors of amidohydrolases can serve as therapeutic agents for treating various diseases, such as cancer, viral infections, and neurodegenerative disorders.

VibH Is an Amide Synthase Homologous to Nonribosomal Peptide Synthetase Condensation Domains". Biochemistry. 39 (50): 15514. ...
... amide synthases). The systematic name of this enzyme class is 4-methylene-L-glutamate:ammonia ligase (AMP-forming). This enzyme ... Winter HC, Su TZ, Dekker EE (1983). "4-methyleneglutamine synthetase: a new amide synthetase present in germinating peanuts" ( ...
... amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (AMP-forming). Other names in common ...
... amide synthases). The systematic name of this enzyme class is glutathionylspermidine:glutathione ligase (ADP-forming). The ... Targeting trypanothione synthase could be a novel way of preventing and curing these diseases through disruption of the ... Evidence for this regulation is that the residues which allow the synthase domain to block the amidase active site are highly ... The main function of trypanothione synthase is to use the free energy generated from ATP hydrolysis to conjugate glutathione ...
... amide synthases). The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine ligase (ADP- ... In enzymology, a glutathionylspermidine synthase (EC 6.3.1.8) is an enzyme that catalyzes the chemical reaction glutathione + ...
... amide synthases). The systematic name of this enzyme class is D-aspartate:[beta-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L- ...
... amide synthases). The systematic name of this enzyme class is L-glutamate:putrescine ligase (ADP-forming). Other names in ...
... amide synthases). The systematic name of this enzyme class is deamido-NAD+:ammonia ligase (AMP-forming). Other names in common ... In enzymology, a NAD+ synthase (EC 6.3.1.5) is an enzyme that catalyzes the chemical reaction ATP + deamido-NAD+ + NH3 ⇌ {\ ... use include NAD+ synthetase, NAD+ synthase, nicotinamide adenine dinucleotide synthetase, and diphosphopyridine nucleotide ...
... amide synthases). The systematic name of this enzyme class is L-aspartate:ammonia ligase (ADP-forming). Other names in common ...
... amide synthases). The systematic name of this enzyme class is L-glutamate:ethylamine ligase (ADP-forming). Other names in ...
... peptide-alpha-amide synthetase, synthase, peptide alpha-amide, peptide alpha-amidating enzyme, peptide alpha-amide synthase, ... Bradbury AF, Finnie MD, Smyth DG (1982). "Mechanism of C-terminal amide formation by pituitary enzymes". Nature. 298 (5875): ...
... adenylosuccinate synthase MeSH D08.811.464.259.200 - amide synthases MeSH D08.811.464.259.200.200 - aspartate-ammonia ligase ... riboflavin synthase MeSH D08.811.913.225.825 - spermidine synthase MeSH D08.811.913.225.912 - spermine synthase MeSH D08.811. ... carbamoyl-phosphate synthase (ammonia) MeSH D08.811.464.259.400 - carbon-nitrogen ligases with glutamine as amide-n-donor MeSH ... nitric oxide synthase type i MeSH D08.811.682.664.500.772.500 - nitric oxide synthase type ii MeSH D08.811.682.664.500.772.750 ...
N-acyl amide synthase genes are found enriched in gastrointestinal bacteria and the lipids, that they encode, interact with ... C21H40O4 by the presence of an amide instead of an ester, and from OEA: C20H39NO2 by the presence of an additional ethanol ...
In all, rifA-E assemble a linear undecaketide and are followed by rifF, which encodes an amide synthase and causes the ... "RifH" encodes aminoDAHP synthase that catalyzes the condensation between 1-deoxy-1-imino-d-erythrose 4-phosphate and ... RifA through rifE encode a type I polyketide synthase module, with the loading module being a non-ribosomal peptide synthetase ... Other types of genes seem to perform post-synthase modifications of the original polyketide. Lepetit introduced Rifampicin, an ...
Glutamate synthase (Fd-GOGAT and NADH-GOGAT) transfer the amide group onto a 2-oxoglutarate molecule producing two glutamates. ... Lea, P. J.; Miflin, B. J. (2003). "Glutamate synthase and the synthesis of glutamate in plants". Plant Physiology and ... In the chloroplasts, glutamine synthetase incorporates this ammonia as the amide group of glutamine using glutamate as a ... Ammonia (both absorbed and synthesized) is incorporated into amino acids via the glutamine synthetase-glutamate synthase (GS- ...
The amidotransferase domain is responsible for removal of the amide nitrogen from the glutamine substrate. The class I ... GMP synthase forms a tetramer in an open box shape, which is a dimer of dimers. The R interfaces are held together with a ... GMP synthase is the second step in the generation of GMP from IMP; the first step occurs when IMP dehydrogenase generates XMP, ... GMP synthase is also involved in amino acid metabolism because it generates L-glutamate from L-glutamine. This enzyme is widely ...
It is composed of a nitrothiazole-ring and a salicylic acid moiety which are linked together by an amide bond ... NTZ is ... In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It ... Gehring U, Arnon DI (1972). "Purification and properties of -ketoglutarate synthase from a photosynthetic bacterium". J. Biol. ...
... which is where the catalysis of amide bond formation takes place. This structure is positioned similarly to the aminoacyl ... Cyclodipeptide synthases (CDPSs) are a newly defined family of peptide-bond forming enzymes that are responsible for the ... "Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide ... "Cyclodipeptide synthases are a family of tRNA-dependent peptide bond-forming enzymes". Nature Chemical Biology. 5 (6): 414-420 ...
The hydroperoxy ligand deprotonates the amide which then closes the β-lactam ring by a nucleophilic attack at the thioaldehyde ... L-cysteinyl-D-valine synthase (ACV synthase). This allows for the binding of the substrate ACV to the deprotonated thiol group ... Isopenicillin N synthase (IPNS) is a non-heme iron protein belonging to the 2-oxoglutarate (2OG)-dependent dioxygenases ... The active sites of most isopenicillin N synthases contain an iron ion. This enzyme is also called isopenicillin N synthetase. ...
Nid is coordinated to two cysteine molecules and two backbone amide compounds, and is in a square-planar coordination. The ... Acetyl-CoA synthase (ACS), not to be confused with Acetyl-CoA synthetase or Acetate-CoA ligase (ADP forming), is a nickel- ... Acetyl-CoA Synthase (ACS) and carbon monoxide dehydrogenase (CODH) are integral enzymes in this one pathway and can perform ... The recommended name for this enzyme is CO-methylating acetyl-CoA synthase. In nature, there are six different pathways where ...
Intramolecular amide N-alkylation of alpha-haloacetamide amides 8 with ethanolic potassium hydroxide using ultrasonication gave ... In general, they arise by the action of a tRNA-dependent cyclodipeptide synthases, a type of enzyme responsible for creating a ... Commonly, an isonitrile is chosen to give a labile terminal amide to enable cyclization. For example, the direct 2,5-DKP ring ... 2,5-Diketopiperazines are typically prepared by one of three methods: amide bond formation, N-alkylation and C-acylation. Most ...
It is then converted with 8-methyl-6-nonenoic acid into capsaicin by the enzyme capsaicin synthase. Acylation of vanillylamine ... using Schotten-Baumann reactions can provide amide derivatives. Examples include nonivamide (a component of some pepper sprays ...
... synthase, glutamate synthase (NADPH), glutamate synthetase (NADP), glutamine amide-2-oxoglutarate aminotransferase ( ... Glutamate synthase (NADH) Glutamate synthase (ferredoxin) Temple SJ, Vance CP, Gantt JS (1998). "Glutamate synthase and ... NADPH-dependent glutamate synthase, NADPH-glutamate synthase, and NADPH-linked glutamate synthase. As of late 2007, only one ... In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction L-glutamine + 2- ...
It has no degrading action on amide, plasminogen and casein. In addition, hementerin inhibits platelet aggregation induced by ... Inhibition is probably achieved by enhanced nitric oxide synthase activity. Calcium is a cofactor (ligand) in this activity. ...
"Structure of an amide bond forming F(420):gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non- ... ribosomal peptide synthases". Journal of Molecular Biology. 372 (2): 456-69. doi:10.1016/j.jmb.2007.06.063. PMC 2678844. PMID ...
"Structure of an amide bond forming F(420):gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non- ... ribosomal peptide synthases". Journal of Molecular Biology. 372 (2): 456-69. doi:10.1016/j.jmb.2007.06.063. PMC 2678844. PMID ...
The gene ann1 encodes an ATP-dependent amide synthetase and is predicted to condense the amine of the C5N group with the ... The ann2 gene encodes a 5-aminolevulinate synthase which condenses glycine and succinyl-CoA in a Claisen-like reaction to form ... Genes ann4 and ann5 are the polyketide synthase part of the biosynthesis. Gene ann4 is organized in four modules, including the ... Annimycin (4-(Z)-annimycin) is a polyenoic acid amide natural product produced by Streptomyces calvus. Annimycin inhibits the ...
Nickel amide, Ni(NH2)2 is a deep red compound that contains Ni6 clusters surrounded by 12 NH2 groups. Nickel amide also forms a ... CO-methylating acetyl-CoA synthase contains two active nickel atoms, one is held in a square planar coordination by two ... Other homoleptic nickel amides derived by substituting the hydrogen atoms are Ni[N(C6H5)2]2 (diphenyl) and boryl amides Ni[ ... cysteine and two amide groups, and the other nickel is held by three sulfur atoms. It is used to catalyse the reduction of ...
... is an orally active thromboxane synthase inhibitor. It has shown a significant clinical improvement in patients with ... Hydrolysis of the amide function completes the synthesis of dazoxiben. Belch, J. J.; Cormie, J.; Newman, P.; McLaren, M.; ...
This enzyme is also called 5-hydroxy-N-methylpyroglutamate synthase. Hersh LB (1970). "5-hydroxy-N-methylpyroglutamate ... specifically in linear amides. The systematic name of this enzyme class is N-methyl-2-oxoglutaramate methylamidohydrolase. ...
VibH Is an Amide Synthase Homologous to Nonribosomal Peptide Synthetase Condensation Domains". Biochemistry. 39 (50): 15514. ...
... amide synthases). The systematic name of this enzyme class is 4-methylene-L-glutamate:ammonia ligase (AMP-forming). This enzyme ... Winter HC, Su TZ, Dekker EE (1983). "4-methyleneglutamine synthetase: a new amide synthetase present in germinating peanuts" ( ...
Amide Synthases. *Amidohydrolases. *Amino Acid Oxidoreductases. *Amino Acid Substitution. *Amino Acids, Branched-Chain ...
... via an amide bond catalyzed by the LAG ONE HOMOLOGUE (LOH) Cer synthases LOH1, LOH2, and LOH3 in Arabidopsis (Markham et al. ... Some fungi use sphinganine-analog mycotoxins (SAMs) to destroy Cer synthase function in plants; therefore, Cer synthases seem ... 2016). GLUCOSYLCERAMIDE SYNTHASE (GCS) transfers a glucose residue from UDP-glucose to a hCer to produce GlcCer via beta- ... 2011). The class II Cer synthases LOH1 and LOH3 prefer to use very-long-chain fatty acids (VLCFAs, more than 18 carbons in ...
An amide synthetase, SfaP, catalyzes the amidation of (2S)-2-ethylmalonyl in a SfaO-dependent manner. Then, a ß-ketoacyl-ACP ... This macrolide is a result of a hybrid polyketide synthase (PKS)-nonribosomal peptide synthetase (NRPS) assembly line that ... synthase III-like protein, SfaN, transfers resultant (2S)-2-ethylmalonamyl from SfaO onto the loading ACP domain of the hybrid ...
Peptide Synthases. Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between ... A 27-amino acid peptide with histidine at the N-terminal and isoleucine amide at the C-terminal. The exact amino acid ... DNA analogs containing neutral amide backbone linkages composed of aminoethyl glycine units instead of the usual phosphodiester ... Formyl PeptidePeptide PHIPeptide SynthasesPeptide HydrolasesReceptors, PeptideAtrial Natriuretic FactorEpitopesProtein ...
Relation of nicotinic acid and nicotinic acid amide to canine black tongue. J Am Chem Soc. 1937. 59:1767-68. ... It is able to scavenge oxygen radicals and to inhibit nitric oxide synthase mRNA induction in activated macrophages. ... Niacin is a pyridine carboxylic acid that is converted into an amide in the body. ...
Farnesyl Diphosphate Synthase *Farnesyltransferase *Fatty Acid Amide Hydrolase *Fatty Acid Synthase *Uncategorized ...
Cesium Carbonate-Catalyzed Reduction of Amides with Hydrosilanes. Wei-Long Xie, Meng-Di Zhao, and Chun-Ming Cui. ... Molecular Drug Resistance Prediction for Acetohydroxyacid Synthase Mutants Against Chlorsulfuron Using MB-QSAR.Yin-Wu He, Cong- ... Copper-Catalyzed N-Methylation of Amides and O-Methylation of Carboxylic Acids by Using Peroxides as the Methylating Reagents. ... A Novel Synthesis of Imides by C-H Functionalization of Aldehydes with Secondary Amides under Palladium Catalysis. Yong-Jun ...
Molecular basis for multiple resistance to acetolactate synthase-inhibiting herbicides and atrazine in Amaranthus blitoides ( ... to ureas and amides (B. tectorum and Alopecurus myosuroides), to synthetic auxins (E. crus-galli) and more recently to the ... Inhibition of Acetolactate Synthase ( HRAC Group 2 (Legacy B). PSII inhibitors - Serine 264 Binders ( HRAC Group 5 (Legacy C1 ... biotypes that evolved resistance to either acetolactate synthase (ALS) inhibitors (A. retroflexus, SuR), to triazine herbicides ...
Farnesyl Diphosphate Synthase *Farnesyltransferase *Fatty Acid Amide Hydrolase *Fatty Acid Synthase *Uncategorized ...
Farnesyl Diphosphate Synthase *Farnesyltransferase *Fatty Acid Amide Hydrolase *Fatty Acid Synthase *Uncategorized ...
ATP Synthase, alpha-Subunit, C-Terminal Fragment 200 g $130.00 058-53 ATP Synthase, Subunit F, C-Terminal 200 g $130.00 ... APGW amide (Lymnae stagnalis) 500 g $55.00 078-09 Apidaecin 1 & 2 Gene peptide (Asn-13-Leu) 500 g $130.00 ...
Glucagon Like Peptide 1 (GLP-1, amide, human) - FAM labeled. *Glycogen Synthase derived peptide - (5-TAMRA) labeled ...
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Recognition of the terminal carboxylate group of the peptide is conferred by a cradle of main chain amides provided by a Gly- ... Other PDZ domains form homotypic dimers: the PDZ domain of the neuronal enzyme nitric oxide synthase binds to the PDZ domain of ... SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE. ... neuronal nitric oxide synthase, and several dystrophin-associated proteins, collectively known as syntrophins. Many PDZ domain- ...
3okf (Cl: 7) - 2.5 Angstrom Resolution Crystal Structure of 3-Dehydroquinate Synthase (Arob) From Vibrio Cholerae Other atoms: ... 3oj8 (Cl: 1) - Alpha-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Contraints ...
Structural basis of catalysis in the bacterial monoterpene synthases linalool synthase and 1,8-cineole synthase. Karuppiah, V. ... Amyl nitrite-mediated conversion of aromatic and heteroaromatic primary amides to carboxylic acids. Potter, G., Miller, G., ...
Samples were loaded into the UPLC system (Ultimate 3000, Thermo Fisher Scientific, USA) equipped with a BEH amide column (1.7 ... by NO synthase. Its reported that in acute liver injury, NO had the ability to oxidase lipids, proteins and DNA, promoting ...
Many of these molecules are produced through non-ribosomal peptide synthase (NRPS) and/or polyketide synthase (PKS) enzymatic ... displaying amide NH signals (δH7.40-7.90), CαH signals (δH3.5-4.7), aliphatic CH2 (δH1.1-1.3) and CH3 signals (δH0.7-0.9). ...
Effect of Alpha-lipoic acid amide on hexachlorobenzene porphyria. Biochem Mol Biol Int 1999;47:815-23. View abstract. ... loss of Akt-dependent endothelial nitric oxide synthase phosphorylation and partial restoration by (R)-alpha-lipoic acid. ...
cellular amide metabolic process. IEP. Enrichment. BP. GO:0043604. amide biosynthetic process. IEP. Enrichment. ... tryptophan synthase activity. IEP. Enrichment. MF. GO:0005198. structural molecule activity. IEP. Enrichment. ...
2C) at 120 h were found to be lower at 0 h. Sucrose synthase gene OsRSUS1 (Fig. 2D) and fructose synthase gene OsFRK-2 (Fig. 2E ... Biotic Stress Related Functions of Hydroxycinnamic Acid Amide in Plants. J Plant Biol. 2015;58:156-63. ... The expression level of raffinose synthase gene Os01g0170000 and galactitol synthase gene OsGolS1 in M. oryzae-infected MoSDT1- ... sucrose synthase gene OsRSUS1 and fructose synthase gene OsFRK-2 in MoSDT1-transgenic rice were significantly higher at late ...
GlcCer Synthase Inhibitor Development. *Acceptor Analog-based GSL Inhibitor Development. *GPI Anchor Inhibitor Development *Dol ... Fatty Amide Analysis Services. *Glycerolipid Analysis Services *Monoacylglycerol Analysis. *Diacylglycerol Analysis. * ...
Nucleophilic strike by Ser195 on the amide carbonyl band of the substrate leads to the forming of a tetrahedral intermediate, ... is crucial for the inhibitory activities of Cav-1 against endothelial nitric oxide synthase (eNOS), which inhibits NO creation ... which is normally stabilized by main-chain amides in the oxyanion gap for binding the oxyanion. A proton from His57 is donated ... the MSC-based prostacyclin synthase gene attenuates pulmonary hypertension and improves prognosis [15]. Let-7a-modified MSCs ...
This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage ... Protein Kinase A Opposes the Phosphorylation-dependent Recruitment of Glycogen Synthase Kinase 3beta to A-kinase Anchoring ...
G. Dong, L. Cao, U. Ryde (2018) "Insight into the reaction mechanism of lipoyl synthase: A QM/MM study, J. Biol. Inorg. Chem, ... "Structure and energetics of ligand-fluorine interactions with galectin-3 backbone and side-chain amides - insight into ... K. P. Jensen, U. Ryde (2003) "Conversion of homocysteine to methionine by methionine synthase: a density functional study", J. ... cluster in biotin synthase", J. Biol. Inorg. Chem., 15. 203-212; DOI: 10.1007/s00775-009-0585-6. ...
  • In addition, coronary blood flow in Langendorff-perfused hearts was evaluated in the presence or absence of nitric oxide synthase (NOS) inhibitor. (biomedcentral.com)
  • Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase. (rhea-db.org)
  • Glutamate synthase is a complex iron-sulfur flavoprotein that catalyzes the reductive transfer of the L-glutamine amide group to C(2) of 2-oxoglutarate, forming two molecules of L-glutamate. (rhea-db.org)
  • To address the problem of the intramolecular electron pathway, we have measured the midpoint potential values of the flavin cofactors and of the 3Fe-4S cluster of glutamate synthase in the isolated alpha and beta subunits and in the alphabeta holoenzyme. (rhea-db.org)
  • BACKGROUND: Combined fatty acid amide hydrolase (FAAH) and cyclooxygenase (COX) inhibition is a promising approach for pain-relief. (cnr.it)
  • DNA analogs containing neutral amide backbone linkages composed of aminoethyl glycine units instead of the usual phosphodiester linkage of deoxyribose groups. (lookformedical.com)
  • The monomers are linked via amide linkages between the γ-carboxyl and the amino group of monomers γ-PGA is a non-toxic, biodegradable polymer. (frontiersin.org)
  • 4-methyleneglutamine synthetase: a new amide synthetase present in germinating peanuts" (PDF). (wikipedia.org)
  • As structural analogs of PABA, sulfon-amides inhibit dihydropteroate synthase and folate production. (brainkart.com)
  • Furthermore, HBPA was found to reduce the protein expression of inducible NO synthase and cyclooxygenase‑2 in macrophages and compared with nialamide, it was established to have more potent radical scavenging activity. (spandidos-publications.com)
  • N,N-dicyclohexylcarbodiimide (DCCD), which forms a covalent bond with the remarkably conserved carboxylic acid of the proteolipid subunit (subunit c) is a well-known inhibitor of the F0F1-ATP synthase. (sdhanjiang.com)
  • This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. (cusabio.com)
  • There are other, non-ribosomal peptide biosynthesis ( PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT ) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. (lookformedical.com)
  • This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-ammonia (or amine) ligases (amide synthases). (wikipedia.org)
  • The DCC, which is an organic soluble carbodiimide, permits the linkage for the amine functionality of the chiral ligand NAS to the carboxy group of the monolithic surface forming a stable amide linkage. (sdhanjiang.com)
  • In this study, we evaluated the effects of caffeic acid phenethyl amide (CAPA) on glucose homeostasis and vascular function in streptozotocin (STZ)-induced type 1 diabetic rats. (biomedcentral.com)
  • Enzymes that catalyze the joining of either ammonia or an amide with another molecule, in which the linkage is in the form of a carbon-nitrogen bond. (nih.gov)
  • Nitric oxide is produced by the following NO synthase (NOS) enzymes: neuronal NOS (nNOS) and endothelial NOS (eNOS,) which are constitutive enzyme isoforms, [ 76 , 77 ] and inducible NOS (iNOS), which is overexpressed in airway epithelial and inflammatory cells of patients with asthma. (medscape.com)
  • Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate. (nih.gov)
  • Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. (nih.gov)
  • For the amide form of nicotinic acid, scientists devised the words 'nicotinamide' and 'niacinamide. (empowerpharmacy.com)
  • A common feature of all EGF-like domains is that they are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase). (embl.de)