An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
A class of enzymes that catalyze oxidation-reduction reactions of amino acids.
A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
An oxidoreductase that catalyzes the oxidative DEAMINATION of GLYCINE to glyoxylate and AMMONIA in the presence of NAD. In BACTERIA lacking transaminating pathways the enzyme can act in the reverse direction to synthesize glycine from glyoxylate and ammonia and NADH.
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
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)
The rate dynamics in chemical or physical systems.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Cold-adapted alanine dehydrogenases from two antarctic bacterial strains: gene cloning, protein characterization, and comparison with mesophilic and thermophilic counterparts. (1/60)

The genes encoding NAD(+)-dependent alanine dehydrogenases (AlaDHs) (EC from the Antarctic bacterial organisms Shewanella sp. strain Ac10 (SheAlaDH) and Carnobacterium sp. strain St2 (CarAlaDH) were cloned and expressed in Escherichia coli. Of all of the AlaDHs that have been sequenced, SheAlaDH exhibited the highest level of sequence similarity to the AlaDH from the gram-negative bacterium Vibrio proteolyticus (VprAlaDH). CarAlaDH was most similar to AlaDHs from mesophilic and thermophilic Bacillus strains. SheAlaDH and CarAlaDH had features typical of cold-adapted enzymes; both the optimal temperature for catalytic activity and the temperature limit for retaining thermostability were lower than the values obtained for the mesophilic counterparts. The k(cat)/K(m) value for the SheAlaDH reaction was about three times higher than the k(cat)/K(m) value for VprAlaDH, but it was much lower than the k(cat)/K(m) value for the AlaDH from Bacillus subtilis. Homology-based structural models of various AlaDHs, including the two psychotropic AlaDHs, were constructed. The thermal instability of SheAlaDH and CarAlaDH may result from relatively low numbers of salt bridges in these proteins.  (+info)

Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional L-alanine dehydrogenase. (2/60)

The 40 kDa antigen of Mycobacterium tuberculosis is the first antigen reported to be present in the pathogenic M. tuberculosis, but not in the vaccine strain Mycobacterium bovis BCG. It is a functional L-alanine dehydrogenase (EC and hence one of the few antigens possessing an enzymic activity. This makes the 40 kDa antigen attractive for potential diagnostic and therapeutic interventions. Recently, we developed a strategy to purify quantities of the recombinant protein in active form, and here we describe the biochemical properties of this enzyme. In the oxidative-deamination reaction, the enzyme showed K(m) values of 13. 8 mM and 0.31 mM for L-alanine and NAD(+), respectively, in a random-ordered mechanism. K(m, app) values in the reductive-amination reaction are 35.4 mM, 1.45 mM and 98.2 microM for ammonium, pyruvate and NADH, respectively. The enzyme is highly specific for all of its substrates in both directions. The pH profile indicates that oxidative deamination virtually may not occur at physiological pH. Hence L-alanine most likely is the product of the reaction catalysed in vivo. The enzyme is heat-stable, losing practically no activity at 60 degrees C for several hours.  (+info)

Structure and mechanism of proton-translocating transhydrogenase. (3/60)

Recent developments have led to advances in our understanding of the structure and mechanism of action of proton-translocating (or AB) transhydrogenase. There is (a) a high-resolution crystal structure, and an NMR structure, of the NADP(H)-binding component (dIII), (b) a homology-based model of the NAD(H)-binding component (dI) and (c) an emerging consensus on the position of the transmembrane helices (in dII). The crystal structure of dIII, in particular, provides new insights into the mechanism by which the energy released in proton translocation across the membrane is coupled to changes in the binding affinities of NADP(+) and NADPH that drive the chemical reaction.  (+info)

Disruption of aldA influences the developmental process in Myxococcus xanthus. (4/60)

Previously, we identified a gene (aldA) from Myxococcus xanthus, which we suggested encoded the enzyme alanine dehydrogenase on the basis of similarity to known Ald protein sequences (M. J. Ward, H. Lew, A. Treuner-Lange, and D. R. Zusman, J. Bacteriol. 180:5668-5675, 1998). In this study, we have confirmed that aldA does encode a functional alanine dehydrogenase, since it catalyzes the reversible conversion of alanine to pyruvate and ammonia. Whereas an aldA gene disruption mutation did not significantly influence the rate of growth or spreading on a rich medium, AldA was required for growth on a minimal medium containing L-alanine as the major source of carbon. Under developmental conditions, the aldA mutation caused delayed aggregation in both wild-type (DZ2) and FB (DZF1) strains. Poorly formed aggregates and reduced levels of spores were apparent in the DZ2 aldA mutant, even after prolonged development.  (+info)

Protein-coding genes as molecular markers for ecologically distinct populations: the case of two Bacillus species. (5/60)

Bacillus globisporus and Bacillus psychrophilus are one among many pairs of ecologically distinct taxa that are distinguished by very few nucleotide differences in 16S rRNA gene sequence. This study has investigated whether the lack of divergence in 16S rRNA between such species stems from the unusually slow rate of evolution of this molecule, or whether other factors might be preventing neutral sequence divergence at 16S rRNA as well as every other gene. B. globisporus and B. psychrophilus were each surveyed for restriction-site variation in two protein-coding genes. These species were easily distinguished as separate DNA sequence clusters for each gene. The limited ability of 16S rRNA to distinguish these species is therefore a consequence of the extremely slow rate of 16S rRNA evolution. The present results, and previous results involving two Mycobacterium species, demonstrate that there exist closely related species which have diverged long enough to have formed clearly separate sequence clusters for protein-coding genes, but not for 16S rRNA. These results support an earlier argument that sequence clustering in protein-coding genes could be a primary criterion for discovering and identifying ecologically distinct groups, and classifying them as separate species.  (+info)

Reassessment of major products of N2 fixation by bacteroids from soybean root nodules. (6/60)

NH3/ was the principal product from soybean bacteroids, prepared by various procedures, when assayed in solution in a flow chamber under N2 fixation conditions. In addition, small quantities of alanine were produced (reaching 20% of NH3/ under some conditions). Some 15N was assimilated by bacteroids purified from soybean root nodules on Percoll density gradients and shaken with 15N2 and 0.008 atm O2. Under these conditions, accounted for 93% of the (15)N fixed into the soluble fraction. This fraction contained no measurable [15N]alanine. Neither these bacteroids nor those prepared by the previously used differential centrifugation method, when incubated with exogenous alanine under non-N2-fixing conditions, gave rise to NH3 from alanine. Therefore, contamination of bacteroid preparations with enzymes of plant cytosolic origin and capable of producing NH3 from alanine cannot explain the failure to detect [15N]alanine [as reported elsewhere: Waters, J. K., Hughes, B. L., II, Purcell, L. C., Gerhardt, K. O., Mawhinney, T. P. & Emerich, D. W. (1998). Proc Natl Acad Sci USA 95, 12038-12042]. Cell-free extracts of the bacteroids as used in the 15N experiments contained alanine dehydrogenase and were able to produce alanine from pyruvate and. Other experiments with alanine dehydrogenase in extracts of cultured rhizobia and bacteroids are reported and discussed in relation to the 15N experiments. Possible reasons for the differences between laboratories regarding the role of alanine are discussed. It is concluded that NH3 is the principal soluble product of N2 fixation by suspensions of soybean bacteroids ex planta and that should continue to be considered the principal product of N2 fixation which is assimilated in vivo in soybean nodules.  (+info)

Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. (7/60)

The events involved in the establishment of a latent infection with Mycobacterium tuberculosis are not fully understood, but hypoxic conditions are generally believed to be the environment encountered by the pathogen in the central part of the granuloma. The present study was undertaken to provide insight into M. tuberculosis protein expression in in vitro latency models where oxygen is depleted. The response of M. tuberculosis to low-oxygen conditions was investigated in both cellular and extracellular proteins by metabolic labeling, two-dimensional electrophoresis, and protein signature peptide analysis by liquid chromatography-mass spectrometry. By peptide mass fingerprinting and immunodetection, five proteins more abundant under low-oxygen conditions were identified from several lysates of M. tuberculosis: Rv0569, Rv2031c (HspX), Rv2623, Rv2626c, and Rv3841 (BfrB). In M. tuberculosis culture filtrates, two additional proteins, Rv0363c (Fba) and Rv2780 (Ald), were found in increased amounts under oxygen limitation. These results extend our understanding of the hypoxic response in M. tuberculosis and potentially provide important insights into the physiology of the latent bacilli.  (+info)

Mycobacterium smegmatis L-alanine dehydrogenase (Ald) is required for proficient utilization of alanine as a sole nitrogen source and sustained anaerobic growth. (8/60)

NAD(H)-dependent L-alanine dehydrogenase (EC (Ald) catalyzes the oxidative deamination of L-alanine and the reductive amination of pyruvate. To assess the physiological role of Ald in Mycobacterium smegmatis, we cloned the ald gene, identified its promoter, determined the protein expression levels, and analyzed the combined effects of nutrient supplementation, oxygen availability, and growth stage on enzyme activity. High Ald activities were observed in cells grown in the presence of L- or D-alanine regardless of the oxygen availability and growth stage. In exponentially growing cells under aerobic conditions, supplementation with alanine resulted in a 25- to 50-fold increase in the enzyme activity. In the absence of alanine supplementation, 23-fold-higher Ald activities were observed in cells grown exponentially under anaerobic conditions. Furthermore, M. smegmatis ald null mutants were constructed by targeted disruption and were shown to lack any detectable Ald activity. In contrast, the glycine dehydrogenase (EC (Gdh) activity in mutant cells remained at wild-type levels, indicating that another enzyme protein is responsible for the physiologically relevant reductive amination of glyoxylate. The ald mutants grew poorly in minimal medium with L-alanine as the sole nitrogen source, reaching a saturation density 100-fold less than that of the wild-type strain. Likewise, mutants grew to a saturation density 10-fold less than that of the wild-type strain under anaerobic conditions. In summary, the phenotypes displayed by the M. smegmatis ald mutants suggest that Ald plays an important role in both alanine utilization and anaerobic growth.  (+info)

Alanine Dehydrogenase (ADH) is an enzyme that catalyzes the reversible conversion between alanine and pyruvate with the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This reaction plays a role in the metabolism of amino acids, particularly in the catabolism of alanine.

In humans, there are multiple isoforms of ADH that are expressed in different tissues and have different functions. The isoform known as ALDH4A1 is primarily responsible for the conversion of alanine to pyruvate in the liver. Deficiencies or mutations in this enzyme can lead to a rare genetic disorder called 4-hydroxybutyric aciduria, which is characterized by elevated levels of 4-hydroxybutyric acid in the urine and neurological symptoms.

Amino acid oxidoreductases are a class of enzymes that catalyze the reversible oxidation and reduction reactions involving amino acids. They play a crucial role in the metabolism of amino acids by catalyzing the interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing a cofactor such as NAD(P)+ or FAD.

The reaction catalyzed by these enzymes can be represented as follows:

L-amino acid + H2O + Coenzyme (Oxidized) → α-keto acid + NH3 + Coenzyme (Reduced)

Amino acid oxidoreductases are classified into two main types based on their cofactor requirements and reaction mechanisms. The first type uses FAD as a cofactor and is called amino acid flavoprotein oxidoreductases. These enzymes typically catalyze the oxidative deamination of L-amino acids to form α-keto acids, ammonia, and reduced FAD. The second type uses pyridine nucleotides (NAD(P)+) as cofactors and is called amino acid pyridine nucleotide-dependent oxidoreductases. These enzymes catalyze the reversible interconversion of L-amino acids to their corresponding α-keto acids, while simultaneously reducing or oxidizing NAD(P)H/NAD(P)+.

Amino acid oxidoreductases are widely distributed in nature and play important roles in various biological processes, including amino acid catabolism, nitrogen metabolism, and the biosynthesis of various secondary metabolites. Dysregulation of these enzymes has been implicated in several diseases, including neurodegenerative disorders and cancer. Therefore, understanding the structure, function, and regulation of amino acid oxidoreductases is crucial for developing novel therapeutic strategies to treat these diseases.

Alanine racemase is an enzyme that catalyzes the conversion of the amino acid alanine between its two stereoisomeric forms, D-alanine and L-alanine. This enzyme plays a crucial role in the biosynthesis of peptidoglycan, a major component of bacterial cell walls. In humans, alanine racemase is found in the cytosol of many tissues, including the liver, kidneys, and brain. It is also an important enzyme in the metabolism of amino acids and has been implicated in various disease processes, including neurodegenerative disorders and cancer.

Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.

Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.

In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.

Glycine dehydrogenase, also known as glycine cleavage system protein P or glycine synthase, is a mitochondrial enzyme complex that plays a crucial role in the catabolism of glycine, an amino acid. This enzyme complex is composed of four separate proteins (P-protein, H-protein, T-protein, and L-protein) that work together to catalyze the reversible conversion of glycine into ammonia, carbon dioxide, and a molecule of 5,10-methylenetetrahydrofolate.

The reaction can be summarized as follows:

Glycine + Tetrahydrofolate + NAD+ ↔ Ammonia + Carbon Dioxide + Methylenetetrahydrofolate + NADH

This pathway is essential for the metabolism of glycine, and its dysfunction has been linked to several genetic disorders, such as non-ketotic hyperglycinemia, which can result in neurological impairments and other health issues.

Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.

In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, ... alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. T Alanine dehydrogenase contains both a N-terminus and C- ... Alanine dehydrogenase (EC is an enzyme that catalyzes the chemical reaction L-alanine + H2O + NAD+ ⇌ {\displaystyle \ ... OConnor RJ, Halvorson H (March 1961). "The substrate specificity of L-alanine dehydrogenase". Biochimica et Biophysica Acta. ...
Timeline for Protein L-alanine dehydrogenase from c.23.12.2: L-alanine dehydrogenase-like: *Protein L-alanine dehydrogenase ... L-alanine dehydrogenase. *Protein L-alanine dehydrogenase from c.23.12.2: L-alanine dehydrogenase-like appears in SCOP 1.71. * ... L-alanine dehydrogenase-like appears in SCOP 1.75. *Protein L-alanine dehydrogenase from c.23.12.2: L-alanine dehydrogenase- ... More info for Protein L-alanine dehydrogenase from c.23.12.2: L-alanine dehydrogenase-like. ...
Gamma-glutamyl Transpeptidase, Alanine Aminopeptidase, and Lactate Dehydrogenase. GGT, AAP, and LDH are brush border enzymes ...
L-ALANINE DEHYDROGENASE COMPLEXED WITH PYRUVATE Coordinates. PDB Format Method. X-RAY DIFFRACTION 2.10 Å. Oligo State. homo- ... Baker, P.J. et al., Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. Nat.Struct. ...
The blood of all the patients was tested with LIOFeron®TB/LTBI assay, containing MTB alanine dehydrogenase, able to ...
Alanine dehydrogenase 2 (Ald2). Q99TF4. 1.86 ↓. 7. Phenylalanine--tRNA ligase α subunit (PheS). P68848. 1.55 ↓. ... Pyruvate dehydrogenase E1 component subunit β (PdhB). P99063. 1.84 ↓. 2.23 ↓. 12. Dihydrolipoyl dehydrogenase (PdhD). P99084. ... Glyceraldehyde-3-phosphate dehydrogenase 1 (GapA1). P99136. 1.62 ↓. * the arrow denotes the direction of regulation; ↑ up- and ... Glyceraldehyde-3-phosphate dehydrogenase 1 (GapA1). P99136. 1.5 ↓. 16. 3-hexulose-6-phosphate synthase (HPS). Q7A774. 1.92 ↓. ...
Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus ... Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus ... Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus ... Conversion of phenylpyruvate to l-phenylalanine by immobilized Clostridium butyricum-alanine dehydrogenase-Micrococcus luteus ...
Elevated levels of aspartate aminotransferase, alanine aminotransferase, and lactate dehydrogenase. Absence of other causes. ...
L-alanine dehydrogenase homologue. *. Species Rhodospirillum rubrum [TaxId:1085] [63938] (4 PDB entries). ... Family c.2.1.4: Formate/glycerate dehydrogenases, NAD-domain [51830] (10 proteins). this domain interrupts the other domain ...
... and lactate dehydrogenase (LDH), were also evaluated. The hierarchization score of the protective effect of pharmacological ... M. Ruscak, H. Hager, and J. Orlicky, "Alanine formation and alanine aminotransferase activity in the nerve tissue with ... alanine aminotransferase (ALT), and lactate dehydrogenase (LDH), were also evaluated. The hierarchization score of the ... Alanine Aminotransferase (ALT/GPT) Activity Assay. ALT enzymatic activity was assessed in 100 μL of the supernatant using the ...
... alanine aminotransferase, and lactate dehydrogenase. Thirteen patients were hospitalized, and none died. Twenty-two patients ...
Elevated levels of lactate dehydrogenase, alanine aminotransferase, and hepatic transaminase. * Elevated creatine kinase level ... Laboratory features - Including marked lymphopenia and leukocytosis, elevated lactate dehydrogenase level, hepatitis, high SARS ...
We focused on Aspartate transaminase (AST), Alanine transaminase (ALT), Lactate dehydrogenase (LDH), Creatine kinase (CK), ...
Markerless deletion of putative alanine dehydrogenase genes in Bacillus licheniformis using a codBA-based counterselection ...
Pre: Before transplantation; NP: Normal plasma control; ALT: Alanine transaminase; LDH: Lactate dehydrogenase; FFP: Fresh ... Pre: Before transplantation; FFP: Fresh frozen plasma; ALT: Alanine transaminase; LDH: Lactate dehydrogenase; ADAMTS13: A ...
... lactate dehydrogenase, aspartate transaminase, alanine transaminase, alkaline phosphatase, total protein, albumin, calcium, ...
Sedimentation, Triglycerides, Total cholesterol, Alanine aminotransferase, Lactate dehydrogenase, C-reactive protein, Na+, K+, ...
... alanine aminotransferase, lactate dehydrogenase, creatinine kinase, alkaline phosphatatse, gamma-glutamyl-transferase, sodium, ...
... lactate dehydrogenase, triglycerides, alanine transaminase (ALT), and fibrinogen, central nervous system involvement, ... Typical laboratory abnormalities include pancytopenia, increased levels of ferritin, liver enzymes, lactate dehydrogenase, ...
... alanine aminotransferase, bilirubin, lactate dehydrogenase, activated partial thromboplastin time (APTT), prothrombin complex, ...
... indicating a very low level of residual activity of lactate dehydrogenase (LDH) and alanine transaminase, whereas all other ... alanine or citrate. In fact, for both methods we detected 1% labeled lactate and 3% labeled alanine, ...
... alanine aminotransferase and 3-hydroxyacy1 CoA dehydrogenase. However a significant increase in the proportion of fast twitch ... Similarly no changes were found in the activities of the following enzymes: lactate dehydrogenase, aldolase, citrate synthase, ...
... lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, gamma-glutamyl transpeptidase, alkaline ... lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, gamma-glutamyl transpeptidase, alkaline ... In the high dose, lower triglyceride levels (males, females), reduced lactate dehydrogenase (LDH) activity (males, females), ... reduced lactate dehydrogenase (LDH) activity (-51% in week 13), decreased phosphate levels (-9% in week 4, -10% in week 13). ...
Isolation and characterization of Phenyl Alanine Ammonia Lyase Gene and Cinnamyl Alcohol Dehydrogenase Gene from hard and soft ...
... lactate dehydrogenase, alanine aminotransferase and aspartate aminotransferase levels. Enzyme levels peaked on the second day ...
  • 7. Beta-alanine suppresses heat inactivation of lactate dehydrogenase. (
  • Thirteen patients had mild serum elevations of liver enzymes aspartase aminotransferase, alanine aminotransferase, and lactate dehydrogenase. (
  • Clinical characteristics as well as serial alanine aminotransferase, aspartate aminotransferase, and lactate dehydrogenase levels were collected. (
  • SFN intervention significantly reduced the EE-induced lactate dehydrogenase (LDH), creatine kinase (CK), alanine aminotransferase (ALT), and aspartate aminotransferase (AST) in the serum, as well as attenuating liver tissue morphological abnormality, oxidative stress injury, and inflammation. (
  • There was no change in the urinary excretion of either albumin or the enzymes N-acetyl-glucosaminidase, lactate dehydrogenase, alanine aminopeptidase and alkaline phosphatase. (
  • Inflammasome activation and pyroptosis of VK2/E6E7 cells were analyzed using microscopy, Hoechst 33342/propidium iodide staining, lactate dehydrogenase release assay, gene and protein expression, co-immunoprecipitation, immunofluorescence, and enzyme-linked immunosorbent assay. (
  • The activity of: alanine aminotransferase (ALT), aspartate aminotranferase (AST), lactate dehydrogenase (LDH), lipase, amylase-as well as the glucose levels were determined after 4 months. (
  • Elevated bilirubin , alanine transaminase and lactate dehydrogenase concentrations are indicative of hepatocellular injury. (
  • Biochemical indices such as aspartate and alanine amino transferases, and lactate dehydrogenase activities, uric acid, complete blood count, and Beta -2-microglubulin were assessed in serum. (
  • The results exhibited an increase in serum lactate dehydrogenase (LDH), aspartate transaminase (AST), and alanine transaminase (ALT) levels compared to control groups. (
  • Alanine aminotransferase and sorbitol dehydrogenase activities were significantly increased in 2,000 ppm males and females. (
  • Activities of alanine aminotransferase (ALT) and isocitrate dehydrogenase (ICD) were statistically increased in both sexes of rats exposed to 800 ppm DMF at all time points. (
  • Left cervical lymphadenopathy and liver inflammation (as evidenced by elevated aspartate aminotransferase and alanine aminotransferase levels) were observed, and IM was suspected. (
  • In the corticosteroid-treated group the maternal platelet count significantly increased (p = 0.006), whereas lactic dehydrogenase and alanine aminotransferase significantly decreased over time (p = 0.03 and p = 0.005) in comparison to the 13 women who did not receive corticosteroids. (
  • Stabilization and significant improvement in the laboratory and clinical parameters associated with HELLP syndrome occurred in women who received high-dose antenatal corticosteroids, as measured by maternal platelet count, urinary output, lactic dehydrogenase, alanine aminotransferase, and postponement of delivery. (
  • In contrast, protein expression of alanine transaminase, aspartate transaminase, glutamate dehydrogenase, and two glutamate transporters was not affected by COM. (
  • Methods: To evaluate the activity of P. perfoliatum against chemical liver injury, levels of alanine transaminase, lactic dehydrogenase, aspartate transaminase, superoxide dismutase, glutathione peroxidase and malondialdehyde were measured, alongside histological assessments of the liver, heart and kidney tissue. (
  • Activities of serum sorbitol dehydrogenase (SDH) were statistically increased in male and female rats (200 to 800 ppm) on study days 4, 24, and 91 (13 weeks). (
  • Three-Dimensional Structures of Apo- and Holo-L-Alanine Dehydrogenase from Mycobacterium Tuberculosis Reveal Conformational Changes Upon Coenzyme Binding. (
  • The triglyceride levels and glutamate dehydrogenase (GLDH) activity were significantly elevated to similar degrees at both time points. (
  • The systematic name of this enzyme class is L-alanine:NAD+ oxidoreductase (deaminating). (
  • Other names in common use include AlaDH, L-alanine dehydrogenase, NAD+-linked alanine dehydrogenase, alpha-alanine dehydrogenase, NAD+-dependent alanine dehydrogenase, alanine oxidoreductase, and NADH-dependent alanine dehydrogenase. (
  • Alanine dehydrogenase (EC is an enzyme that catalyzes the chemical reaction L-alanine + H2O + NAD+ ⇌ {\displaystyle \rightleftharpoons } pyruvate + NH3 + NADH + H+ The 2 substrates of this enzyme are L-alanine, water, and nicotinamide adenine dinucleotide+ because water is 55M and does not change, whereas its 4 products are pyruvate, ammonia, NADH, and hydrogen ion. (
  • An NAD -dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA . (
  • The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. (
  • It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer. (
  • Дефіцит глюкозо-6-фосфат-дегідрогенази (Г6ФДГ) Glucose-6-phosphate dehydrogenase (G6PD) deficiency is an X-linked enzymatic defect common in people with African ancestry that can result in hemolysis after acute illnesses or intake of oxidant. (