Aspartate-Semialdehyde Dehydrogenase: An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.Aspartate Kinase: An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.Homoserine Dehydrogenase: An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.Succinate-Semialdehyde Dehydrogenase: An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).Methylmalonate-Semialdehyde Dehydrogenase (Acylating): An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.Aldehyde Oxidoreductases: Oxidoreductases that are specific for ALDEHYDES.Brain Diseases, Metabolic, Inborn: Brain disorders resulting from inborn metabolic errors, primarily from enzymatic defects which lead to substrate accumulation, product reduction, or increase in toxic metabolites through alternate pathways. The majority of these conditions are familial, however spontaneous mutation may also occur in utero.4-Aminobutyrate Transaminase: An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.Hydroxybutyrate DehydrogenaseAminomuconate-Semialdehyde Dehydrogenase: An NAD+ dependent enzyme that catalyzes the oxidation of 2-aminomuconate 6-semialdehyde to 2-aminomuconate.Sodium Oxybate: The sodium salt of 4-hydroxybutyric acid. It is used for both induction and maintenance of ANESTHESIA.Amino Acid Metabolism, Inborn Errors: Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.Aldehyde Dehydrogenase: An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.Aspartate Aminotransferases: Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.Hydroxybutyrates: Salts and esters of hydroxybutyric acid.Glutamate-5-Semialdehyde Dehydrogenase: An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.Succinates: Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.Adipates: Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.GlutaratesEnzyme-Linked Immunosorbent Assay: An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Structural Homology, Protein: The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Templates, Genetic: Macromolecular molds for the synthesis of complementary macromolecules, as in DNA REPLICATION; GENETIC TRANSCRIPTION of DNA to RNA, and GENETIC TRANSLATION of RNA into POLYPEPTIDES.Computer Graphics: The process of pictorial communication, between human and computers, in which the computer input and output have the form of charts, drawings, or other appropriate pictorial representation.Neisseria meningitidis, Serogroup W-135: Strains of Neisseria meningitidis found mostly in Africa.Arsenic: A shiny gray element with atomic symbol As, atomic number 33, and atomic weight 75. It occurs throughout the universe, mostly in the form of metallic arsenides. Most forms are toxic. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), arsenic and certain arsenic compounds have been listed as known carcinogens. (From Merck Index, 11th ed)Carbon-Nitrogen Ligases with Glutamine as Amide-N-Donor: Enzymes that catalyze the joining of glutamine-derived ammonia and another molecule. The linkage is in the form of a carbon-nitrogen bond. EC 6.3.5.EstersGlutaminaseRibonucleotide ReductasesAdenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Fragaria: A plant genus of the family ROSACEAE known for the edible fruit.Aldehydes: Organic compounds containing a carbonyl group in the form -CHO.Rosa: A plant genus in the family ROSACEAE and order Rosales. This should not be confused with the genus RHODIOLA which is sometimes called roseroot.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Retinal Dehydrogenase: A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.Methionine: A sulfur-containing essential L-amino acid that is important in many body functions.Molecular Sequence Data: 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.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.Gene Expression Profiling: The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.Herpestidae: The family of agile, keen-sighted mongooses of Asia and Africa that feed on RODENTS and SNAKES.Osteochondrodysplasias: Abnormal development of cartilage and bone.Gene Expression Regulation, Plant: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Pentachlorophenol: An insecticide and herbicide that has also been used as a wood preservative. Pentachlorphenol is a widespread environmental pollutant. Both chronic and acute pentachlorophenol poisoning are medical concerns. The range of its biological actions is still being actively explored, but it is clearly a potent enzyme inhibitor and has been used as such as an experimental tool.Chloranil: A quinone fungicide used for treatment of seeds and foliage.Chlorophenols: Phenols substituted with one or more chlorine atoms in any position.Sulfhydryl Compounds: Compounds containing the -SH radical.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Kinetics: The rate dynamics in chemical or physical systems.

An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. (1/46)

We have determined the kinetic parameters of the individual steps of the threonine pathway from aspartate in Escherichia coli under a single set of experimental conditions chosen to be physiologically relevant. Our aim was to summarize the kinetic behaviour of each enzyme in a single tractable equation that takes into account the effect of the products as competitive inhibitors of the substrates in the forward reaction and also, when appropriate (e.g. near-equilibrium reactions), as substrates of the reverse reactions. Co-operative feedback inhibition by threonine and lysine was also included as necessary. We derived the simplest rate equations that describe the salient features of the enzymes in the physiological range of metabolite concentrations in order to incorporate them ultimately into a complete model of the threonine pathway, able to predict quantitatively the behaviour of the pathway under natural or engineered conditions.  (+info)

Threonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics. (2/46)

We have developed an experimental model of the whole threonine pathway that allows us to study the production of threonine from aspartate under different conditions. The model consisted of a desalted crude extract of Escherichia coli to which we added the substrates and necessary cofactors of the pathway: aspartate, ATP and NADPH. In this experimental model we measured not only the production of threonine, but also the time dependence of all the intermediate metabolites and of the initial substrates, aspartate, ATP and NADPH. A stoichiometric conversion of precursors into threonine was observed. We have derived conditions in which a quasi steady state can be transiently observed and used to simulate physiological conditions of functioning of the pathway in the cell. The dependence of threonine synthesis and of the aspartate and NADPH consumption on the initial aspartate and threonine concentrations exhibits greater sensitivity to the aspartate concentration than to the threonine concentration in these non-steady-state conditions. A response to threonine is only observed in a narrow concentration range from 0.23 to 2 mM.  (+info)

Control of the threonine-synthesis pathway in Escherichia coli: a theoretical and experimental approach. (3/46)

A computer simulation of the threonine-synthesis pathway in Escherichia coli Tir-8 has been developed based on our previous measurements of the kinetics of the pathway enzymes under near-physiological conditions. The model successfully simulates the main features of the time courses of threonine synthesis previously observed in a cell-free extract without alteration of the experimentally determined parameters, although improved quantitative fits can be obtained with small parameter adjustments. At the concentrations of enzymes, precursors and products present in cells, the model predicts a threonine-synthesis flux close to that required to support cell growth. Furthermore, the first two enzymes operate close to equilibrium, providing an example of a near-equilibrium feedback-inhibited enzyme. The predicted flux control coefficients of the pathway enzymes under physiological conditions show that the control of flux is shared between the first three enzymes: aspartate kinase, aspartate semialdehyde dehydrogenase and homoserine dehydrogenase, with no single activity dominating the control. The response of the model to the external metabolites shows that the sharing of control between the three enzymes holds across a wide range of conditions, but that the pathway flux is sensitive to the aspartate concentration. When the model was embedded in a larger model to simulate the variable demands for threonine at different growth rates, it showed the accumulation of free threonine that is typical of the Tir-8 strain at low growth rates. At low growth rates, the control of threonine flux remains largely with the pathway enzymes. As an example of the predictive power of the model, we studied the consequences of over-expressing different enzymes in the pathway.  (+info)

Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'. (4/46)

The first two genes of the lysine pathway are closely linked forming a transcriptional operon in the cephamycin producer 'Amycolatopsis lactamdurans'. The asd gene, encoding the enzyme aspartic semialdehyde dehydrogenase, has been cloned by complementation of Escherichia coli asd mutants. It encodes a protein of 355 aa with a deduced M(r) of 37109. The ask gene encoding the aspartokinase (Ask) is located upstream of the asd gene as shown by determination of Ask activity conferred to E. coli transformants. asd and ask are separated by 2 nt and are transcribed in a bicistronic 2.6 kb mRNA. As occurs in corynebacteria, the presence of a ribosome-binding site within the ask sequence suggests that this ORF encodes two overlapping proteins, Askalpha of 421 aa and M(r) 44108, and Askbeta of 172 aa and M(r) 18145. The formation of both subunits of Ask from a single gene (ask) was confirmed by using antibodies against the C-terminal end of Ask which is identical in both subunits. Ask activity of 'A. lactamdurans' is regulated by the concerted action of lysine plus threonine and this inhibition is abolished in E. coli transformants containing Ser(301) to Tyr, or Gly(345) to Asp mutations of the 'A. lactamdurans' ask gene.  (+info)

A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. (5/46)

L-Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes the reductive dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde in the aspartate biosynthetic pathway of plants and micro-organisms. The aspartate pathway produces fully one-quarter of the naturally occurring amino acids, but is not found in humans or other eukaryotic organisms, making ASADH an attractive target for the development of new antibacterial, fungicidal, or herbicidal compounds. We have determined the structure of ASADH from Vibrio cholerae in two states; the apoenzyme and a complex with NADP, and a covalently bound active site inhibitor, S-methyl-L-cysteine sulfoxide. Upon binding the inhibitor undergoes an enzyme-catalyzed reductive demethylation leading to a covalently bound cysteine that is observed in the complex structure. The enzyme is a functional homodimer, with extensive intersubunit contacts and a symmetrical 4-amino acid bridge linking the active site residues in adjacent subunits that could serve as a communication channel. The active site is essentially preformed, with minimal differences in active site conformation in the apoenzyme relative to the ternary inhibitor complex. The conformational changes that do occur result primarily from NADP binding, and are localized to the repositioning of two surface loops located on the rim at opposite sides of the NADP cleft.  (+info)

Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene. (6/46)

Metabolites such as diaminopimelate and some aromatic derivatives, not synthesized in mammalian cells, are essential for growth of bacteria. As a first step towards the design of a new human live vaccine that uses attenuated strains of Leptospira interrogans, the asd, aroD and dapD genes, encoding aspartate beta-semialdehyde dehydrogenase, 3-dehydroquinase and tetrahydrodipicolinate N-succinyltransferase, respectively, were cloned by complementation of Escherichia coli mutants. The complete nucleotide sequence of the asd gene was determined and found to contain an open reading frame capable of encoding a protein of 349 amino acids with a calculated Mr of 38,007. Comparison of this deduced L. interrogans aspartate beta-semialdehyde dehydrogenase amino acid sequence with those of the same enzyme from Saccharomyces cerevisiae and Corynebacterium glutamicum revealed 46% and 36% identity, respectively. By contrast, the identity between the L. interrogans enzyme and the Streptococcus mutans or E. coli enzymes was less than 31%. Highly conserved sequences within aspartate semialdehyde dehydrogenase from the five organisms were observed at the amino and carboxyl termini, and around the cysteine of the active site.  (+info)

Mechanism of action of an antifungal antibiotic, RI-331, (S) 2-amino-4-oxo-5-hydroxypentanoic acid; kinetics of inactivation of homoserine dehydrogenase from Saccharomyces cerevisiae. (7/46)

An antifungal antibiotic (S) 2-amino-4-oxo-5-hydroxypentanoic acid, inhibited the biosynthesis of the aspartate family of amino acids (methionine, isoleucine and threonine) followed by the inhibition of protein biosynthesis in Saccharomyces cerevisiae. This inhibition was effected by impeding the biosynthesis of their common intermediate precursor, homoserine. The inhibition of biosynthesis of homoserine by the antibiotic was attributable to inactivation of homoserine dehydrogenase [EC 1.1.1.3], which is involved in the conversion of aspartate semialdehyde to homoserine in the metabolic pathway leading to threonine, methionine and isoleucine. Since such enzymic activity is not present in animal cells, the selective antifungal activity of the antibiotic is thus explained.  (+info)

Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase. (8/46)

The structural analysis of an enzymatic reaction intermediate affords a unique opportunity to study a catalytic mechanism in extraordinary detail. Here we present the structure of a tetrahedral intermediate in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Haemophilus influenzae at 2.0-A resolution. ASADH is not found in humans, yet its catalytic activity is required for the biosynthesis of essential amino acids in plants and microorganisms. Diaminopimelic acid, also formed by this enzymatic pathway, is an integral component of bacterial cell walls, thus making ASADH an attractive target for the development of new antibiotics. This enzyme is able to capture the substrates aspartate-beta-semialdehyde and phosphate as an active complex that does not complete the catalytic cycle in the absence of NADP. A distinctive binding pocket in which the hemithioacetal oxygen of the bound substrate is stabilized by interaction with a backbone amide group dictates the R stereochemistry of the tetrahedral intermediate. This pocket, reminiscent of the oxyanion hole found in serine proteases, is completed through hydrogen bonding to the bound phosphate substrate.  (+info)

*Threonine

... aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase. Threonine ... Threonine is synthesized from aspartate in bacteria such as E. coli. In the genetic code it is encoded by the codons ACU, ACC, ... In humans the gene for threonine dehydrogenase is an inactive pseudogene, so threonine it is converted to α-ketobutyrate. The ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...

*Burkholderia pseudomallei

Aspartate-β-semialdehyde dehydrogenase (asd) gene deletion mutants are auxotrophic for diaminopimelate (DAP) in rich media and ...

*Asd RNA motif

Finally, although the asd gene encodes an enzyme, aspartate-semialdehyde dehydrogenase, that participates in the synthesis of ...

*ASD

... may refer to: ASD (database) Asd RNA motif Aspartate-semialdehyde dehydrogenase Acute stress disorder, a psychiatric ...

*Methionine

Aspartokinase Aspartate-semialdehyde dehydrogenase Homoserine dehydrogenase Homoserine O-transsuccinylase Cystathionine-γ- ... The intermediate aspartate-semialdehyde is the branching point with the lysine biosynthetic pathway, where it is instead ... 7) The enzyme α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine by two reduction steps of the terminal carboxyl ...

*Succinic semialdehyde dehydrogenase deficiency

The major ionotropic glutamine receptors include the N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methylisoxazole-4- ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency. From Wikipedia, the free encyclopedia. (Redirected from Gamma-hydroxybutyric ...

*Homoserine dehydrogenase

... catalyzes the reaction of aspartate-semialdehyde (ASA) to homoserine. The overall reaction reduces the ... Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta- ... At night, aspartate is converted to asparagine for storage. Additionally, the aspartate kinase-homoserine dehydrogenase gene is ... Homoserine dehydrogenase and aspartate kinase are both subject to significant regulation (refer to figure 3). HSD is inhibited ...

*Aspartate-semialdehyde dehydrogenase

Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta- ... and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes. This ...

*Succinic semialdehyde dehydrogenase deficiency

The major ionotropic glutamine receptors include the N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methylisoxazole-4- ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Pearl, P. L.; Novotny, E. J.; Acosta, M. T.; Jakobs, C.; Gibson, K. M. (2003). "Succinic semialdehyde dehydrogenase deficiency ...

*Amino acid synthesis

Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ... β-aspartate semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine kinase, threonine synthase. The biosynthesis of ... The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase. These ... Oxaloacetate/aspartate: lysine, asparagine, methionine, threonine, and isoleucine[edit]. The oxaloacetate/aspartate family of ...

*Malonate-semialdehyde dehydrogenase (acetylating)

This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine ... In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical ... V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry. 235: 589-594. PMID ... This enzyme is also called malonic semialdehyde oxidative decarboxylase. ...

*Category:Protein pages needing a picture

Aspartate carbamoyltransferase. *Aspartate-semialdehyde dehydrogenase. *Asprosin. *Ataxin 7. *ATCase/OTCase family. *Atg1 ...

*Biosynthesis

Aspartate semialdehyde dehydrogenase catalyzes the NADPH-dependent reduction of aspartyl phosphate to yield aspartate ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase catalyzes the reduction reaction by dephosphorylation of aspartyl-β-phosphate to yield ... aspartate-β-semialdehyde. Dihydrodipicolinate synthase catalyzes the condensation reaction of aspartate-β-semialdehyde with ...

*List of MeSH codes (D08)

... aminomuconate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.374 --- aspartate-semialdehyde dehydrogenase MeSH D08.811. ... succinate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.875 --- succinate-semialdehyde dehydrogenase (NAD(P)+) MeSH ... l-aminoadipate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.812 --- malonate-semialdehyde dehydrogenase (acetylating) ... betaine-aldehyde dehydrogenase MeSH D08.811.682.657.163.562 --- glutamate-5-semialdehyde dehydrogenase MeSH D08.811.682.657. ...

*Carboxynorspermidine synthase

L-aspartate 4-semialdehyde + putrescine + NADPH + H+ The reaction takes place in the opposite direction. Nakao, H.; Shinoda, S ... Carboxynorspermidine synthase (EC 1.5.1.43, carboxynorspermidine dehydrogenase, carboxyspermidine dehydrogenase, CASDH, CANSDH ... L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ (2) carboxyspermidine + H2O + NADP+ ⇌ {\displaystyle \ ...

*Diaminopimelate epimerase

The production of dihydropicolinate from aspartate-semialdehyde controls flux into the lysine/diaminopimelic acid pathway. ... In the third variant, found in some Gram-positive bacteria, a dehydrogenase converts tetrahydropicolinate directly to meso-DAP ... Viola RE (2001). "The central enzymes of the aspartate family of amino acid biosynthesis". Acc. Chem. Res. 34 (5): 339-49. doi: ... The lysine/diaminopimelic acid branch of the aspartate pathway produces the essential amino acid lysine via the intermediate ...

*List of EC numbers (EC 1)

... acetaldehyde dehydrogenase (acetylating) EC 1.2.1.11: aspartate-semialdehyde dehydrogenase EC 1.2.1.12: glyceraldehyde-3- ... lysine 6-dehydrogenase EC 1.4.1.19: tryptophan dehydrogenase EC 1.4.1.20: phenylalanine dehydrogenase EC 1.4.1.21: aspartate ... glutarate-semialdehyde dehydrogenase EC 1.2.1.21: glycolaldehyde dehydrogenase EC 1.2.1.22: lactaldehyde dehydrogenase EC 1.2. ... succinate-semialdehyde dehydrogenase (acylating) EC 1.2.1.77: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) EC 1.2. ...

*Succinic acid

Finally, succinic semialdehyde is oxidized by succinic semialdehyde dehydrogenase (SSADH) to form succinate, re-entering the ... During ischemia, fumarate is formed from purine nucleotide breakdown and partial reversal of the malate/aspartate shuttle. ... Under pathological and physiological conditions, the malate-aspartate shuttle or the purine nucleotide shuttle can increase ... Loss-of-function mutations in the genes encoding succinate dehydrogenase, frequently found in hereditary paraganglioma and ...

*Αr15 RNA

This motif was identified clustering genes of tartrate dehydrogenase, succinate semialdehyde dehydrogenase, 3- ... Aspartate amino transferase and LysR/unknown transcriptional regulator) with partial synteny to the first group. A very ... hydroxyisobutyrate dehydrogenase and hydroxypyruvate isomerase in S. meliloti, and several Rhizobiums and it is marked in the ...

*Protein metabolism

Aspartate → β-aspartate-semialdehyde → Homoserine + lysine Aspartic Acid -OOC-CH2- Oxaloacetate → Aspartic Acid ( ... 3-phosphoglycerate → 3-phosphohydroxypyruvate (3-phosphoglycerate dehydrogenase) → 3-phosphoserine (aminotransferase) → Serine ... Aspartate → β-aspartate-semialdehyde → Homoserine → Threonine Cysteine HS-CH2- Serine → Cystathionine → α-ketobutyrate → ... Glutamate → Glutamate-5-semialdehyde (γ-glutamyl kinase) → Arginine Histidine§. NH-CH=N-CH=C-CH2- Glucose → Glucose-6-phosphate ...

*Fatty acid synthase

2cg5: STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL ... Aspartate carbamoyltransferase. *Dihydroorotase. *Cholesterol side-chain cleavage enzyme. *Cytochrome b6f complex. *Electron ... "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1-3): 94- ...

*Citric acid cycle

... succinate-semialdehyde dehydrogenase. The regulation of the citric acid cycle is largely determined by product inhibition and ... Of these amino acids, aspartate and glutamine are used, together with carbon and nitrogen atoms from other sources, to form the ... inhibits pyruvate dehydrogenase, isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, and also citrate synthase. Acetyl-coA ... It activates pyruvate dehydrogenase phosphatase which in turn activates the pyruvate dehydrogenase complex. Calcium also ...

*Kynureninase

3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... Kynureninase belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ...

*Glycine cleavage system

3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... glycine dehydrogenase (decarboxylating) or just glycine dehydrogenase. L-protein (GCSL or DLD) EC 1.8.1.4 known by many names, ... but most commonly dihydrolipoyl dehydrogenase H-protein (GCSH) is modified with lipoic acid and interacts with all other ...

*Fumaric acid

It is formed by the oxidation of succinate by the enzyme succinate dehydrogenase. Fumarate is then converted by the enzyme ... 2-Amino-3-carboxymuconic semialdehyde. *2-Aminomuconic semialdehyde. *2-Aminomuconic acid. *Glutaryl-CoA ... in eukaryotic organisms from succinate in complex 2 of the electron transport chain via the enzyme succinate dehydrogenase. It ...
Shop Aspartate-semialdehyde dehydrogenase leader peptide ELISA Kit, Recombinant Protein and Aspartate-semialdehyde dehydrogenase leader peptide Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Arsenic atom in PDB 1pqu: Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound With Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate
SWISS-MODEL Template Library (SMTL) entry for 1t4b.1. 1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.
The lysine, threonine, and methionine biosynthetic pathways share the three initial enzymatic steps, which are referred to as the Common Pathway (CP). In Escherichia coli three different aspartokinases (AKI, AKII, AKIII, the products of thrA, metL and lysC, respectively) can perform the first step of the CP. Moreover, two of them (AKI and AKII) are bifunctional, carrying also homoserine dehydrogenasic activity (hom product). The second step of the CP is catalyzed by a single aspartate semialdehyde dehydrogenase (ASDH, the product of asd). Thus, in the CP of E. coli while a single copy of ASDH performs the same reaction for three different metabolic routes, three different AKs perfom a unique step. Why and how such a situation did emerge and maintain? How is it correlated to the different regulatory mechanisms acting on these genes? The aim of this work was to trace the evolutionary pathway leading to the extant scenario in proteobacteria. The analysis of the structure, organization, phylogeny, and
Acupuncture is the practice of placing very thin needles through the skin in specific locations of the body for the purpose of healing and relief of symptoms.
The antileukemic activity of l-asparaginase (ASNase), an important component of therapy for acute lymphoblastic leukemia, is thought to result from depletion of serum l-asparagine (Asn). In studies of the pharmacological effects of ASNase, investigators have reported prolonged reduction in the serum concentration of Asn after the administration of ASNase. Such measurements may not be valid because ASNase present in the blood sample may hydrolyze Asn before its determination. We examined recovery of [U-14C]Asn from blood samples with and without various concentrations of added ASNase. In the presence of ≥0.01 IU/ml of ASNase, the amount of [U-14C]Asn recovered was ,15% of that without ASNase. Utilizing this assay, we studied the effect of 2 known inhibitors of ASNase in an attempt to improve Asn recovery. In the presence of aspartic β semialdehyde (ASA), or 5-diazo-4-oxo-l-norvaline (DONV), and up to 1.0 IU/ml ASNase, Asn levels remained at ,90% of control. ASA prevented the hydrolysis of ...
A novel N-acetyltranferase (NAT) with high specificity for L-dopa was partially purified and characterized during this study. Streptomyces akiyoshiensis NAT was isolated from liquid cultures and the cell free extract was ...
Lysine biosynthesis is one of the unique metabolic capabilities of cyst forming Coccidia such as Toxoplasma gondii and Neospora caninum. Toxoplasma and Neospora genome analysis shows that they have the unique metabolic capability to synthesise lysine, an essential amino acid in humans. This capability is absent in other Apicomplexa. It has been suggested that Toxoplasma can convert aspartate into lysine via diaminopimelate pathway [1]. This pathway takes place via four different routes in different organisms (KEGG Lysine biosynthesis pathway). Of these, three variants belong to different groups of prokaryotes and the plant variant of the pathway was identified recently in Arabidopsis thaliana [2]. The first four enzymes (aspartate kinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase) and the last enzyme (diaminopimelate decarboxylase) is the same in all variants of the pathway and these five enzymes are present in T. gondii and N. caninum ...
Small differences in as many as a thousand genes contribute to risk for autism, according to a study led by Mount Sinai researchers and the Autism Sequencing Consortium (ASC), and published today in the journal Nature.. The new study examined data on several types of rare, genetic differences in more than 14,000 DNA samples from parents, affected children, and unrelated individuals - by far the largest number to date - to dramatically expand the list of genes identified with autism spectrum disorder (ASD).. Most of the genes that contribute to autism remain unknown, but the current study increases the number of definitive autism genes almost fourfold to 33, compared to the 9 genes most closely tied to risk in recent years by similar studies in several labs. It also identified more than 70 additional, likely ASD genes. Each of these genes is mutated in more than 5 percent of individuals with autism, signifying a large, relative contribution to risk for a complex genetic disease.. By casting a ...
Curtiss, R. III, Jagusztyn-Krynicka, E.K., Hansen, J.B., Smorawinska, M., Abiko, Y., and Cardineau, G.A. 1982. Expression of Streptococcus mutans plasmid and chromosomal gene in Escherichia coli K-12. In: Microbial. Drug resistance, S. Mitsuhashi (ed.), Japan Scientific Societies Press, Tokyo and University Park press, Baltimore, Vol. 3, pp. 15-27.. Murchison, H.H., Barrett, J.F., Cardineau, G.A., and Curtiss III, R. 1986. Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs. Infection and Immunity 54: 273-282.. Cardineau, G.A. and Curtiss III, R. 1987. Nucleotide sequence of the asd gene of Streptococcus mutans: identification of the promoter region and evidence for attenuator like sequences preceding the structural gene. J. Biol. Chem.262: 3344-3353.. Adang, M.J., Brody, M., Cardineau, G.A., Eagan, N., Roush, R.T., Shewmaker, C.K., Jones, A., Oakes, J.V., and McBride, K.E. 1993. The construction and expression of a Bacillus thuringiensis cryIIIA gene in ...
The aspartate biosynthetic pathway, essential in plants and in most bacteria and fungi, can produce the amino acids threonine, lysine, methionine, and isoleucine. The first commitment step of this pathway is catalyzed by aspartokinase (AK). The archeal thermophilic Methanococcus jannaschii has only a single, monofunctional form of AK. X-ray crystallographic studies indicate that mjAK is a tetramer in the crystalline state, which coincides with the oligomeric structure in solution. The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK.5 Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. The allosteric inhibitor, L-threonine, cooperatively binds to two sites in each monomer of this dimer of dimers, one site in the regulatory domain interface ...
2013 - Helmholtz Zentrum München - German Research Center for Environmental Health (GmbH) Ingolstädter Landstraße 1, D-85764 Neuherberg, Germany. Disclaimer: MIPS Databases and associated information are protected by copyright. This server and its associated data and services are for academic, non-commercial use only. The Helmholtz Zentrum München has no liability for the use of results, data or information which have been provided through this server. Neither the use for commercial purposes, nor the redistribution of MIPS database files to third parties nor the distribution of parts of files or derivative products to any third parties is permitted.. ...
Residues 1 to 131 (E-value = 9.7e-37) place NG1997 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain (PF01118 ...
6-Phosphogluconate dehydrogenase is a potential target for new drugs against African trypanosomiasis. Phosphorylated aldonic acids are strong inhibitors of 6-phosphogluconate dehydrogenase, and 4-phospho-d-erythronate (4PE) and 4-phospho-d-erythronohydroxamate are two of the strongest inhibitors of the Trypanosoma brucei enzyme. Binding of the substrate 6-phospho-d-gluconate (6PG), the inhibitors 5-phospho-d-ribonate (5PR) and 4PE, and the coenzymes NADP, NADPH and NADP analogue 3-amino-pyridine adenine dinucleotide phosphate to 6-phospho-d-gluconate dehydrogenase from T. brucei was studied using isothermal titration calorimetry. Binding of the substrate (K(d) = 5 microm) and its analogues (K(d) =1.3 microm and K(d) = 2.8 microm for 5PR and 4PE, respectively) is entropy driven, whereas binding of the coenzymes is enthalpy driven. Oxidized coenzyme and its analogue, but not reduced coenzyme, display a half-site reactivity in the ternary complex with the substrate or inhibitors. Binding of 6PG and ...
Background The identification of genetic target genes is a key step for rational engineering of production strains towards bio-based chemicals, fuels or therapeutics. This is often a difficult task,...
SWISS-MODEL Template Library (SMTL) entry for 3hij.1. Crystal structure of dihydrodipicolinate synthase from Bacillus anthracis in complex with its substrate, pyruvate
Glutamate-5-semialdehyde is a non-proteinogenic amino acid involved in the biosynthesis of proline and arginine (via ornithine), as well as in the biosynthesis of antibiotics, such as carbapenems. It is synthesized by the reduction of glutamyl-5-phosphate by glutamate-5-semialdehyde dehydrogenase. Glutamate-1-semialdehyde Baich A (1971). "The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate -semialdehyde dehydrogenase (NADP), the second enzyme in the pathway". Biochim. Biophys. Acta. 244 (1): 129-34. doi:10.1016/0304-4165(71)90129-2. PMID 4399189 ...
Complete information for LYZ gene (Protein Coding), Lysozyme, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
2 For my friends. Aware of how they worry about me and of how terrible I am when it comes to staying in touch, I want them to know that I still feel them lifting me up ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Introduction: Aspartokinase (A1, A2, A3) Homoserine dehydrogenase (B1, B2) Threonine dehydratase (C1, C2) Allosteric regulation of selective isozymes some unregulated Sequential feedback inhibition Same product inhibits its biosynthetic path at multiple sites Inhibits first enzyme in pathway

Aspartate-semialdehyde dehydrogenase leader peptide elisa and antibodyAspartate-semialdehyde dehydrogenase leader peptide elisa and antibody

Recombinant Protein and Aspartate-semialdehyde dehydrogenase leader peptide Antibody at MyBioSource. Custom ELISA Kit, ... Shop Aspartate-semialdehyde dehydrogenase leader peptide ELISA Kit, ... Aspartate-semialdehyde dehydrogenase leader peptide. Aspartate-semialdehyde dehydrogenase leader peptide ELISA Kit. Aspartate- ... semialdehyde dehydrogenase leader peptide Recombinant. Aspartate-semialdehyde dehydrogenase leader peptide Antibody. SMU_988.1 ...
more infohttps://www.mybiosource.com/protein_family.php?root=aspartate-semialdehyde-dehydrogenase-leader-peptide

Arsenic in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus...Arsenic in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus...

Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound With Nadp, S- ... Arsenic in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus ... binding sites of Arsenic atom in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase ...
more infohttp://arsenic.atomistry.com/pdb1pqu.html

IUCr) Acta Crystallographica Section D Volume 68, Part 6, June 2012IUCr) Acta Crystallographica Section D Volume 68, Part 6, June 2012

Crystal structures of aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis in complex with glycerol and with ... PDB references: aspartate-semialdehyde dehydrogenase, complex with SMCS and sulfate, 3tz6; complex with glycerol and sulfate, ... Structures of ternary complexes of aspartate-semi-aldehyde de-hydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv. ...
more infohttp://journals.iucr.org/d/issues/2012/06/00/index.html

KEGG BRITE: Enzymes - Fragaria vesca (woodland strawberry)KEGG BRITE: Enzymes - Fragaria vesca (woodland strawberry)

1.2.1.10 acetaldehyde dehydrogenase (acetylating) 1.2.1.11 aspartate-semialdehyde dehydrogenase 1.2.1.12 glyceraldehyde-3- ... 1.2.1.3 aldehyde dehydrogenase (NAD+) 101298221 aldehyde dehydrogenase family 2 member B4 101311183 aldehyde dehydrogenase ... 101298824 aldehyde dehydrogenase family 7 member A1 K00128 ALDH; aldehyde dehydrogenase (NAD+) [EC:1.2.1.3] K00128 ALDH; ... 101311533 aldehyde dehydrogenase family 3 member H1-like 101313059 aldehyde dehydrogenase family 3 member H1-like 101310892 ...
more infohttp://www.genome.jp/kegg-bin/get_htext?fve01000+101313059

Succinic semialdehyde dehydrogenase deficiency - WikipediaSuccinic semialdehyde dehydrogenase deficiency - Wikipedia

The major ionotropic glutamine receptors include the N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methylisoxazole-4- ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency. From Wikipedia, the free encyclopedia. (Redirected from Gamma-hydroxybutyric ...
more infohttps://en.wikipedia.org/wiki/Gamma-hydroxybutyric_aciduria

MetReconIssues | Systems Biology Research GroupMetReconIssues | Systems Biology Research Group

2003). "Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643." J Biol Chem 278( ... prediction and experimental verification of the gene encoding the NAD+/NADP+-dependent succinate semialdehyde dehydrogenase in ... this same step converting aspartate to imminoaspartate is replaced by a non-homologous NAD-dependent enzyme(Yang, Savchenko et ...
more infohttp://systemsbiology.ucsd.edu/InSilicoOrganisms/OtherOrganisms/MetReconIssues

Aspartate-semialdehyde dehydrogenase - WikipediaAspartate-semialdehyde dehydrogenase - Wikipedia

Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta- ... and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5 UTR of some Asd genes. This ...
more infohttps://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase

RCSB PDB - Protein Feature View 









 - Aspartate-semialdehyde dehydrogenase - Q51344 (DHAS PSEAE)RCSB PDB - Protein Feature View - Aspartate-semialdehyde dehydrogenase - Q51344 (DHAS PSEAE)

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. UniProt ... Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ...
more infohttp://www.rcsb.org/pdb/protein/Q51344

asd - Aspartate-semialdehyde dehydrogenase - Shigella flexneri - asd gene & proteinasd - Aspartate-semialdehyde dehydrogenase - Shigella flexneri - asd gene & protein

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ...
more infohttps://www.uniprot.org/uniprot/P0A9R1

asd - Aspartate-semialdehyde dehydrogenase - Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12) - asd gene...asd - Aspartate-semialdehyde dehydrogenase - Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12) - asd gene...

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ... Aspartate-semialdehyde dehydrogenase (asd). *Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional ... Aspartate-semialdehyde dehydrogenase (asd). *Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional ... Aspartate-semialdehyde dehydrogenase (asd). *Dihydrodipicolinate synthase (dapA-1), 4-hydroxy-tetrahydrodipicolinate synthase ( ...
more infohttps://www.uniprot.org/uniprot/Q56734

RCSB PDB - 3Q1L: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine...RCSB PDB - 3Q1L: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine...

Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently ... Aspartate beta-semialdehyde dehydrogenase. A, B, C, D. 366. Streptococcus pneumoniae (strain ATCC BAA-255 / R6). Mutation(s): 0 ... Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently ... An early pathway enzyme, l-aspartate-β-semialdehyde dehydrogenase, produces a key intermediate at the first branch point of ...
more infohttps://www.rcsb.org/structure/3Q1L

Aspartate-semialdehyde dehydrogenase elisa and antibodyAspartate-semialdehyde dehydrogenase elisa and antibody

Recombinant Protein and Aspartate-semialdehyde dehydrogenase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Aspartate-semialdehyde dehydrogenase 1. Aspartate-semialdehyde dehydrogenase 1 ELISA Kit. Aspartate-semialdehyde dehydrogenase ... Aspartate-semialdehyde dehydrogenase 2. Aspartate-semialdehyde dehydrogenase 2 ELISA Kit. Aspartate-semialdehyde dehydrogenase ... Aspartate-semialdehyde dehydrogenase. Aspartate-semialdehyde dehydrogenase ELISA Kit. Aspartate-semialdehyde dehydrogenase ...
more infohttps://www.mybiosource.com/proteins-family/aspartate-semialdehyde-dehydrogenase

Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV...Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV...

... was identified as the aspartate semialdehyde dehydrogenase gene (asd), encoding a polypeptide of 346 amino acids. Subclones ... Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV- ... Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase ... Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV- ...
more infohttps://www.semanticscholar.org/paper/Sequence-analysis-and-expression-of-the-and-operon-Zhang-Jiang/99625e18341f50c53ccd3fcd96774d3bd7d1da71

SWISS-MODEL Template Library | 1t4b.1SWISS-MODEL Template Library | 1t4b.1

1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase. ... in Escherichia coli Aspartate beta-Semialdehyde Dehydrogenase. J.Mol.Biol. (2004) Release Date. 2004-07-13. Peptides. Aspartate ... 1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.. Coordinates. PDB Format Method. X-RAY ...
more infohttps://swissmodel.expasy.org/templates/1t4b

IUCr) Acta Crystallographica Section F Volume 71, Part 11, November 2015IUCr) Acta Crystallographica Section F Volume 71, Part 11, November 2015

The structure of aspartate semialdehyde dehydrogenase (ASADH) from the fungal pathogen C. neoformans has been determined. The ... Cover illustration: Structure of a fungal form of aspartate semi-aldehyde de-hydrogenase from Cryptococcus neoformans (Dahal & ... Structure of a fungal form of aspartate semi-aldehyde de-hydrogenase from Cryptococcus neoformans. ...
more infohttp://journals.iucr.org/f/issues/2015/11/00/

Methionine - New World EncyclopediaMethionine - New World Encyclopedia

β-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine acyltransferase. *cystathionine-γ-synthase. * ... 7) α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a three-step ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene ...
more infohttps://www.newworldencyclopedia.org/entry/Methionine

Threonine - New World EncyclopediaThreonine - New World Encyclopedia

α-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine kinase. *threonine synthase. Threonine ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
more infohttp://www.newworldencyclopedia.org/entry/Threonine

BRENDA - Reference to 1.2.1.11; Id = 654110BRENDA - Reference to 1.2.1.11; Id = 654110

Critical catalytic functional groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase. Blanco, J.; Moore, R.A.; ... L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+ ... soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in ... soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in ...
more infohttps://brenda-enzymes.org/literature.php?e=1.2.1.11&r=654110

SCOPe 2.04: Structural Classification of Proteins - extendedSCOPe 2.04: Structural Classification of Proteins - extended

Compound: aspartate-semialdehyde dehydrogenase. Species: Streptococcus pneumoniae [TaxId:406563]. Gene: CGSSp23BS72_03388. ... Compound: aspartate-semialdehyde dehydrogenase. Species: Streptococcus pneumoniae [TaxId:406563]. Gene: CGSSp23BS72_03388. ... Description: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase complex with NADP and 2-aminoterephthalate. Class ...
more infohttp://scop.berkeley.edu/pdb/code=3pyx&ver=2.04

Nicotinamide adenine dinucleotide phosphate - DrugBankNicotinamide adenine dinucleotide phosphate - DrugBank

Details6. Aspartate-semialdehyde dehydrogenase. Kind. Protein. Organism. Haemophilus influenzae (strain ATCC 51907 / DSM 11121 ... UAspartate-semialdehyde dehydrogenase. Not Available. Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). ... UShikimate dehydrogenase. Not Available. Escherichia coli (strain K12). UNADP-dependent isopropanol dehydrogenase. Not ... Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ...
more infohttps://www.drugbank.ca/drugs/DB03461

SCOPe 2.07: Structural Classification of Proteins - extendedSCOPe 2.07: Structural Classification of Proteins - extended

Compound: aspartate-semialdehyde dehydrogenase. Species: Vibrio cholerae [TaxId:666]. Gene: VC_2036. Database cross-references ... Compound: aspartate-semialdehyde dehydrogenase. Species: Vibrio cholerae [TaxId:666]. Gene: VC_2036. Database cross-references ... Description: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Vibrio Cholerae with product of S-allyl-L- ...
more infohttp://scop.berkeley.edu/pdb/code=3q0e

ThreonineThreonine

α-aspartate semialdehyde dehydrogenase * homoserine dehydrogenase * homoserine kinase * threonine synthase. Metabolism. ... It is converted to pyruvate via Threonine Dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
more infohttps://www.bionity.com/en/encyclopedia/Threonine.html

MethionineMethionine

β-aspartate semialdehyde dehydrogenase * homoserine dehydrogenase * homoserine acyltransferase * cystathionine-γ-synthase * ... 7) α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a three-step ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene ...
more infohttps://www.bionity.com/en/encyclopedia/Methionine.html

Homoserine dehydrogenase - WikipediaHomoserine dehydrogenase - Wikipedia

Homoserine dehydrogenase catalyzes the reaction of aspartate-semialdehyde (ASA) to homoserine. The overall reaction reduces the ... Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta- ... At night, aspartate is converted to asparagine for storage. Additionally, the aspartate kinase-homoserine dehydrogenase gene is ... Homoserine dehydrogenase and aspartate kinase are both subject to significant regulation (refer to figure 3). HSD is inhibited ...
more infohttps://en.wikipedia.org/wiki/Homoserine_dehydrogenase

HOM2 gene cDNA ORF clone, Saccharomyces cerevisiae S288C - GenScriptHOM2 gene cDNA ORF clone, Saccharomyces cerevisiae S288C - GenScript

Next-day shipping cDNA ORF clones derived from HOM2 aspartate-semialdehyde dehydrogenase available at GenScript, starting from ... aspartate-semialdehyde dehydrogenase. Comment. Comment: REVIEWED REFSEQ: This record has been curated by SGD. This record is ... Saccharomyces cerevisiae S288C aspartate-semialdehyde dehydrogenase (HOM2), partial mRNA.. Target ORF information:. Epitope ... Saccharomyces cerevisiae S288C aspartate-semialdehyde dehydrogenase (HOM2), partial mRNA.. pcDNA3.1+/C-(K)DYK or customized ...
more infohttps://www.genscript.com/gene/saccharomyces-cerevisiae-s288c/851736/hom2.html
  • The GABA shunt bypasses two steps (the oxidation of α-ketoglutarate to succinate) of the tricarboxylic acid (TCA) cycle via reactions catalyzed by three enzymes: glutamate decarboxylase, GABA transaminase, and succinic semialdehyde dehydrogenase. (frontiersin.org)
  • Once the C4 carboxylic acid is reduced to an aldehyde and the C1 aldehyde is oxidized to a carboxylic acid, experiments suggest that Asp 219, Glu 208 and a water molecule bind ASA in the active site while Lys 223 donates a proton to the aspartate-semialdehyde C4 oxygen. (wikipedia.org)
  • The second step of the CP is catalyzed by a single aspartate semialdehyde dehydrogenase (ASDH, the product of asd ). (biomedcentral.com)