Lyases
Chondroitin Lyases
Pectobacterium chrysanthemi
Chondroitinases and Chondroitin Lyases
Pectins
Molecular Sequence Data
Amino Acid Sequence
Chicory
Aldehyde-Lyases
Carbon-Oxygen Lyases
Erwinia
Heparin Lyase
Oxo-Acid-Lyases
Cloning, Molecular
Polygalacturonase
Substrate Specificity
Base Sequence
Alginates
Sequence Homology, Amino Acid
Hexuronic Acids
Isocitrate Lyase
Rhodophyta
Phycobilins
Chondroitin ABC Lyase
Sphingomonas
Cytochromes c1
Sequence Alignment
Escherichia coli
Binding Sites
Bacteroides
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Glucuronic Acid
Hevea
Hydrogen-Ion Concentration
Mutation
Glycosaminoglycans
Proteus vulgaris
Uronic Acids
Electrophoresis, Polyacrylamide Gel
Chondroitin Sulfates
Protein Conformation
Protein Structure, Tertiary
Mutagenesis, Site-Directed
Sulfonium Compounds
Protein Binding
Dermatan Sulfate
Models, Molecular
Carbohydrate Sequence
Carbon-Nitrogen Lyases
Carbon-Carbon Lyases
Sequence Analysis, DNA
DNA-(Apurinic or Apyrimidinic Site) Lyase
Crystallography, X-Ray
Recombinant Fusion Proteins
Pseudomonas
Structure-Activity Relationship
N-Glycosyl Hydrolases
Catalysis
Chromatography, Gel
Fungi
Isoenzymes
Plants
DNA Glycosylases
Bacillus
Protein Structure, Secondary
Intramolecular Lyases
Heparitin Sulfate
Biocatalysis
Catalytic Domain
Chromatography, High Pressure Liquid
Temperature
Oligosaccharides
Gene Expression Regulation, Bacterial
Peptide Fragments
Multigene Family
Sequence Homology, Nucleic Acid
Chromatography
Enzyme Stability
Cell Wall
Transfection
Naphthols
Phosphorus-Oxygen Lyases
Conserved Sequence
Plasmids
DNA-Binding Proteins
Chromatography, Ion Exchange
Protein Sorting Signals
Protein Processing, Post-Translational
DNA
Precipitin Tests
Carrier Proteins
Nuclear Proteins
Crystallization
Viral Envelope Proteins
Membrane Proteins
Peptides
Saccharomyces cerevisiae
Ficain
Transcription, Genetic
Viral Matrix Proteins
Nucleocapsid Proteins
Phosphorylation
Mutagenesis
Restriction Mapping
Endopeptidases
Cell Compartmentation
Carbon-Sulfur Lyases
HeLa Cells
Transcription Factors
COS Cells
Cytoplasm
DNA Repair
Saccharomyces cerevisiae Proteins
RNA, Messenger
Fluorescent Antibody Technique
Bluetongue virus
Peptide Mapping
Point Mutation
Virion
Cell Membrane
Repetitive Sequences, Nucleic Acid
Genetic Complementation Test
Cricetinae
Gene Expression
Inclusion Bodies, Viral
DNA, Complementary
Cells, Cultured
Genes
Transmissible gastroenteritis virus
Open Reading Frames
Gene Expression Regulation, Enzymologic
Antigens, Polyomavirus Transforming
Oncogene Protein pp60(v-src)
Gene Deletion
Virus Assembly
Epitope Mapping
Rabbits
Viral Structural Proteins
Cercopithecus aethiops
Protein Biosynthesis
Retroviridae Proteins
Blotting, Western
Rhodamines
Biological Transport
Macromolecular Substances
Amino Acid Substitution
Amino Acids
Cattle
Bacterial Outer Membrane Proteins
Proteins
Amino Acid Motifs
DNA Primers
Cell Nucleus
Immunoblotting
Murine hepatitis virus
Avian Sarcoma Viruses
Tyrosine
Oligodeoxyribonucleotides
Carboxylic Acids
Two-Hybrid System Techniques
Glycoproteins
Protein Kinases
Alternative Splicing
Viral Nonstructural Proteins
Polymerase Chain Reaction
A kinetic study of ribulose bisphosphate carboxylase from the photosynthetic bacterium Rhodospirillum rubrum. (1/1854)
The activation kinetics of purified Rhodospirillum rubrum ribulose bisphosphate carboxylase were analysed. The equilibrium constant for activation by CO(2) was 600 micron and that for activation by Mg2+ was 90 micron, and the second-order activation constant for the reaction of CO(2) with inactive enzyme (k+1) was 0.25 X 10(-3)min-1 . micron-1. The latter value was considerably lower than the k+1 for higher-plant enzyme (7 X 10(-3)-10 X 10(-3)min-1 . micron-1). 6-Phosphogluconate had little effect on the active enzyme, and increased the extent of activation of inactive enzyme. Ribulose bisphosphate also increased the extent of activation and did not inhibit the rate of activation. This effect might have been mediated through a reaction product, 2-phosphoglycolic acid, which also stimulated the extent of activation of the enzyme. The active enzyme had a Km (CO2) of 300 micron-CO2, a Km (ribulose bisphosphate) of 11--18 micron-ribulose bisphosphate and a Vmax. of up to 3 mumol/min per mg of protein. These data are discussed in relation to the proposed model for activation and catalysis of ribulose bisphosphate carboxylase. (+info)A general method for selection of alpha-acetolactate decarboxylase-deficient Lactococcus lactis mutants to improve diacetyl formation. (2/1854)
The enzyme acetolactate decarboxylase (Ald) plays a key role in the regulation of the alpha-acetolactate pool in both pyruvate catabolism and the biosynthesis of the branched-chain amino acids, isoleucine, leucine, and valine (ILV). This dual role of Ald, due to allosteric activation by leucine, was used as a strategy for the isolation of Ald-deficient mutants of Lactococcus lactis subsp. lactis biovar diacetylactis. Such mutants can be selected as leucine-resistant mutants in ILV- or IV-prototrophic strains. Most dairy lactococcus strains are auxotrophic for the three amino acids. Therefore, the plasmid pMC004 containing the ilv genes (encoding the enzymes involved in the biosynthesis of IV) of L. lactis NCDO2118 was constructed. Introduction of pMC004 into ILV-auxotrophic dairy strains resulted in an isoleucine-prototrophic phenotype. By plating the strains on a chemically defined medium supplemented with leucine but not valine and isoleucine, spontaneous leucine-resistant mutants were obtained. These mutants were screened by Western blotting with Ald-specific antibodies for the presence of Ald. Selected mutants lacking Ald were subsequently cured of pMC004. Except for a defect in the expression of Ald, the resulting strain, MC010, was identical to the wild-type strain, as shown by Southern blotting and DNA fingerprinting. The mutation resulting in the lack of Ald in MC010 occurred spontaneously, and the strain does not contain foreign DNA; thus, it can be regarded as food grade. Nevertheless, its application in dairy products depends on the regulation of genetically modified organisms. These results establish a strategy to select spontaneous Ald-deficient mutants from transformable L. lactis strains. (+info)Reconstitution of a bacterial/plant polyamine biosynthesis pathway in Saccharomyces cerevisiae. (3/1854)
Polyamine synthesis in most organisms is initiated by the decarboxylation of ornithine to form putrescine via ornithine decarboxylase (ODC). Plants, some bacteria and some fungi and protozoa generate putrescine from arginine, via arginine decarboxylase (ADC) and agmatine ureohydrolase (AUH) or agmatine iminohydrolase. A polyamine-requiring strain of Saccharomyces cerevisiae with a mutation in the gene encoding ODC was transformed with plasmids bearing genes encoding Escherichia coli ADC and AUH. Transformants regained the ability to grow in the absence of exogenous polyamines and contained enzyme activities consistent with the presence of both prokaryotic enzymes. Similar results were obtained when a plasmid containing a gene encoding oat (Avena sativa L.) ADC was substituted for the E. coli gene. These data demonstrate the successful complementation of a yeast biosynthetic polyamine synthesis defect by genes encoding an alternative pathway found in bacteria; they also show that plant ADC can substitute for the bacterial enzyme in this pathway. The recombinant yeast provides a tool for the study of the functional properties of these enzymes and for discovery of compounds that specifically inhibit this pathway. (+info)Characterization of mdcR, a regulatory gene of the malonate catabolic system in Klebsiella pneumoniae. (4/1854)
The Klebsiella pneumoniae mdcR gene, which encodes a LysR-type regulator, was overexpressed in Escherichia coli. Purified MdcR was found to bind specifically to the control region of either the malonate decarboxylase (mdc) genes or mdcR. We have also demonstrated that MdcR is an activator of the expression of the mdc genes, whereas it represses the transcription of the putative control region of mdcR, PmdcR, indicating a negative autoregulatory control. (+info)Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects. Identification of five novel mutations, one of them causing instability of the protein. (5/1854)
The inherited metabolic disease propionic acidemia (PA) can result from mutations in either of the genes PCCA or PCCB, which encode the alpha and beta subunits, respectively, of the mitochondrial enzyme propionyl CoA-carboxylase. In this work we have analyzed the molecular basis of PCCA gene defects, studying mRNA levels and identifying putative disease causing mutations. A total of 10 different mutations, none predominant, are present in a sample of 24 mutant alleles studied. Five novel mutations are reported here for the first time. A neutral polymorphism and a variant allele present in the general population were also detected. To examine the effect of a point mutation (M348K) involving a highly conserved residue, we have carried out in vitro expression of normal and mutant PCCA cDNA and analyzed the mitochondrial import and stability of the resulting proteins. Both wild-type and mutant proteins were imported into mitochondria and processed into the mature form with similar efficiency, but the mature mutant M348K protein decayed more rapidly than did the wild-type, indicating a reduced stability, which is probably the disease-causing mechanism. (+info)Cyclic AMP can decrease expression of genes subject to catabolite repression in Saccharomyces cerevisiae. (6/1854)
External cyclic AMP (cAMP) hindered the derepression of gluconeogenic enzymes in a pde2 mutant of Saccharomyces cerevisiae, but it did not prevent invertase derepression. cAMP reduced nearly 20-fold the transcription driven by upstream activation sequence (UAS1FBP1) from FBP1, encoding fructose-1,6-bisphosphatase; it decreased 2-fold the activation of transcription by UAS2FBP1. Nuclear extracts from cells derepressed in the presence of cAMP were impaired in the formation of specific UASFBP1-protein complexes in band shift experiments. cAMP does not appear to act through the repressing protein Mig1. Control of FBP1 transcription through cAMP is redundant with other regulatory mechanisms. (+info)Brown adipose tissue triacylglycerol synthesis in rats adapted to a high-protein, carbohydrate-free diet. (7/1854)
Adaptation of rats to a high-protein, carbohydrate-free (HP) diet induced a marked reduction of brown adipose tissue (BAT) fatty acid (FA) synthesis from both 3H2O and [14C]glucose in vivo, with pronounced decreases in the activities of four enzymes associated with lipogenesis: glucose-6-phosphate dehydrogenase, malic enzyme, citrate lyase, and acetyl-CoA carboxylase. In both HP-adapted and control rats, in vivo incorporation of 3H2O and [14C]glucose into BAT glyceride-glycerol was much higher than into FA. It could be estimated that most of the glycerol synthetized was used to esterify preformed FA. Glycerol synthesis from nonglucose sources (glyceroneogenesis) was increased in BAT from HP rats, as evidenced by an increased capacity of tissue fragments to incorporate [1-14C]pyruvate into glycerol and by a fourfold increase in the activity of phosphoenolpyruvate carboxykinase activity, a key glyceroneogenic enzyme. The data suggest that high rates of glyceroneogenesis and of esterification of preformed FA in BAT from HP-adapted rats are essential for preservation of tissue lipid stores, necessary for heat generation when BAT is recruited in nonshivering thermogenesis. (+info)Evidence for an inducible nucleotide-dependent acetone carboxylase in Rhodococcus rhodochrous B276. (8/1854)
The metabolism of acetone was investigated in the actinomycete Rhodococcus rhodochrous (formerly Nocardia corallina) B276. Suspensions of acetone- and isopropanol-grown R. rhodochrous readily metabolized acetone. In contrast, R. rhodochrous cells cultured with glucose as the carbon source lacked the ability to metabolize acetone at the onset of the assay but gained the ability to do so in a time-dependent fashion. Chloramphenicol and rifampin prevented the time-dependent increase in this activity. Acetone metabolism by R. rhodochrous was CO2 dependent, and 14CO2 fixation occurred concomitant with this process. A nucleotide-dependent acetone carboxylase was partially purified from cell extracts of acetone-grown R. rhodochrous by DEAE-Sepharose chromatography. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggested that the acetone carboxylase was composed of three subunits with apparent molecular masses of 85, 74, and 16 kDa. Acetone metabolism by the partially purified enzyme was dependent on the presence of a divalent metal and a nucleoside triphosphate. GTP and ITP supported the highest rates of acetone carboxylation, while CTP, UTP, and XTP supported carboxylation at 10 to 50% of these rates. ATP did not support acetone carboxylation. Acetoacetate was determined to be the stoichiometric product of acetone carboxylation. The longer-chain ketones butanone, 2-pentanone, 3-pentanone, and 2-hexanone were substrates. This work has identified an acetone carboxylase with a novel nucleotide usage and broader substrate specificity compared to other such enzymes studied to date. These results strengthen the proposal that carboxylation is a common strategy used for acetone catabolism in aerobic acetone-oxidizing bacteria. (+info)Some common effects of chromosomal deletions include:
1. Genetic disorders: Chromosomal deletions can lead to a variety of genetic disorders, such as Down syndrome, which is caused by a deletion of a portion of chromosome 21. Other examples include Prader-Willi syndrome (deletion of chromosome 15), and Williams syndrome (deletion of chromosome 7).
2. Birth defects: Chromosomal deletions can increase the risk of birth defects, such as heart defects, cleft palate, and limb abnormalities.
3. Developmental delays: Children with chromosomal deletions may experience developmental delays, learning disabilities, and intellectual disability.
4. Increased cancer risk: Some chromosomal deletions can increase the risk of developing certain types of cancer, such as chronic myelogenous leukemia (CML) and breast cancer.
5. Reproductive problems: Chromosomal deletions can lead to reproductive problems, such as infertility or recurrent miscarriage.
Chromosomal deletions can be diagnosed through a variety of techniques, including karyotyping (examination of the chromosomes), fluorescence in situ hybridization (FISH), and microarray analysis. Treatment options for chromosomal deletions depend on the specific effects of the deletion and may include medication, surgery, or other forms of therapy.
1. Activation of oncogenes: Some viruses contain genes that code for proteins that can activate existing oncogenes in the host cell, leading to uncontrolled cell growth.
2. Inactivation of tumor suppressor genes: Other viruses may contain genes that inhibit the expression of tumor suppressor genes, allowing cells to grow and divide uncontrollably.
3. Insertional mutagenesis: Some viruses can insert their own DNA into the host cell's genome, leading to disruptions in normal cellular function and potentially causing cancer.
4. Epigenetic changes: Viral infection can also cause epigenetic changes, such as DNA methylation or histone modification, that can lead to the silencing of tumor suppressor genes and the activation of oncogenes.
Viral cell transformation is a key factor in the development of many types of cancer, including cervical cancer caused by human papillomavirus (HPV), and liver cancer caused by hepatitis B virus (HBV). In addition, some viruses are specifically known to cause cancer, such as Kaposi's sarcoma-associated herpesvirus (KSHV) and Merkel cell polyomavirus (MCV).
Early detection and treatment of viral infections can help prevent the development of cancer. Vaccines are also available for some viruses that are known to cause cancer, such as HPV and hepatitis B. Additionally, antiviral therapy can be used to treat existing infections and may help reduce the risk of cancer development.
Explanation: Neoplastic cell transformation is a complex process that involves multiple steps and can occur as a result of genetic mutations, environmental factors, or a combination of both. The process typically begins with a series of subtle changes in the DNA of individual cells, which can lead to the loss of normal cellular functions and the acquisition of abnormal growth and reproduction patterns.
Over time, these transformed cells can accumulate further mutations that allow them to survive and proliferate despite adverse conditions. As the transformed cells continue to divide and grow, they can eventually form a tumor, which is a mass of abnormal cells that can invade and damage surrounding tissues.
In some cases, cancer cells can also break away from the primary tumor and travel through the bloodstream or lymphatic system to other parts of the body, where they can establish new tumors. This process, known as metastasis, is a major cause of death in many types of cancer.
It's worth noting that not all transformed cells will become cancerous. Some forms of cellular transformation, such as those that occur during embryonic development or tissue regeneration, are normal and necessary for the proper functioning of the body. However, when these transformations occur in adult tissues, they can be a sign of cancer.
See also: Cancer, Tumor
Word count: 190
Carboxy-lyases
S-adenosyl-L-methionine:(3-phospho-D-glycerate-carboxy-lyase (dimerizing))-lysine 6-N-methyltransferase
Sulfinoalanine decarboxylase
Edith Wilson Miles
Sulfopyruvate decarboxylase
Carnitine decarboxylase
Hydroxypyruvate decarboxylase
Orsellinate decarboxylase
Dihydroxyfumarate decarboxylase
O-pyrocatechuate decarboxylase
Phenylpyruvate decarboxylase
Oxalate decarboxylase
4-hydroxyphenylpyruvate decarboxylase
Stipitatonate decarboxylase
4-oxalocrotonate decarboxylase
Phosphonopyruvate decarboxylase
UDP-glucuronate decarboxylase
David Sidney Feingold
4,5-dihydroxyphthalate decarboxylase
3,4-dihydroxyphthalate decarboxylase
Tartrate decarboxylase
Aspartate 4-decarboxylase
Hydroxyglutamate decarboxylase
Benzoylformate decarboxylase
Gallate decarboxylase
Aminobenzoate decarboxylase
Valine decarboxylase
Acetylenedicarboxylate decarboxylase
Glutaconyl-CoA decarboxylase
EC 4.1.1.102
Oxalyl-CoA decarboxylase
3-oxolaurate decarboxylase
Hexenuronic acid
Indole-3-glycerol-phosphate synthase
UXS1
Methylmalonyl-CoA decarboxylase
Phosphoenolpyruvate carboxylase
Phenylalanine decarboxylase
Fatty acid synthesis
Ribulose-bisphosphate carboxylase)-lysine N-methyltransferase
Carboxynorspermidine decarboxylase
7-carboxy-7-deazaguanine synthase
List of enzymes
Phosphoenolpyruvate carboxykinase (ATP)
6-carboxytetrahydropterin synthase
3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase
FPG IleRS zinc finger
Aconitate decarboxylase
UROD gene: MedlinePlus Genetics
DeCS
Regulation of Growth of Acinetobacter calcoaceticus NCIB8250 on L-Mandelate in Batch Culture | Microbiology Society
Levodopa effect on [|sup|18|/sup|F]fluorodopa influx to brain: Normal volunteers and patients with Parkinson's disease -...
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Adenosylmethionine Decarboxylase | Profiles RNS
PRIME PubMed | Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in...
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What is the Difference Between RuBisCo and PEP Carboxylase - Pediaa.Com
DeCS
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HXT11 - PDC1 | S. cerevisiae SSL interaction - Slorth
Bio2Vec
Are synthase and synthase same?
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Molecules | Free Full-Text | Genetically Encodable Scaffolds for Optimizing Enzyme Function
ECMDB: D-Serine (ECMDB03406) (M2MDB000497)
June | 2020 | GSK3 Inhibitors
Cephalosporin C sodium - Xcess Biosciences
Publication Detail
Malonyl CoA decarboxylase deficiency: C to T transition in intron 2 of the MCD gene - PubMed
Discovery and characterization of gut microbiota decarboxylases that can produce the neurotransmitter tryptamine - PubMed
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DeCS
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Pharos : Target List
Pharos : Target List
NDF-RT Code NDF-RT Name NDF-RT Kind
NEW (2006) MESH HEADINGS WITH SCOPE NOTES (UNIT RECORD FORMAT; 9/3/2005
Publication: Dietary fatty acids modulate associations between genetic variants and circulating …
Classification-Index
TERM
Hyperaldosteronism Differential Diagnoses
Biomarkers Search
Vasopressin-Targets
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Time- and Dose-Related Effects of Di-(2-ethylhexyl) Phthalate and Its Main Metabolites on the Function of the Rat Fetal Testis...
PMID- 3504184
and
Enzymes1
- The CaICL1 gene, which encode the glyoxylate cycles enzymes isocitrate lyase are required for growth on non-fermentable carbon sources. (intechopen.com)
Synthase1
- A synthase is also acknowledged as a lyase that catalyzes the cleavage of various chemical bonds through means excluding hydrolysis and oxidation without demand for any energy, whereas a synthetase is a ligase joining two chemicals or compounds with requirement for energy . (moviecultists.com)
Process1
- Addition of a putative S. cerevisiae ubiquitination site carboxy terminus of CaIcl1 led to galactose- accelerated degradation of this protein in C. albicans cell via a ubiquitin-dependent process. (intechopen.com)