Aldehyde Dehydrogenase
Lyases
Chondroitin Lyases
Pectobacterium chrysanthemi
Chondroitinases and Chondroitin Lyases
Pectins
Aldehyde Reductase
Aldehyde-Lyases
Chicory
Substrate Specificity
Acetaldehyde
Carbon-Oxygen Lyases
Erwinia
Heparin Lyase
Molecular Sequence Data
Oxo-Acid-Lyases
Polygalacturonase
Disulfiram
Amino Acid Sequence
Catalysis
Alginates
Retinal Dehydrogenase
Alcohols
Hexuronic Acids
Isocitrate Lyase
Rhodophyta
Alcohol Oxidoreductases
Phycobilins
Chondroitin ABC Lyase
Sphingomonas
Stereoisomerism
Cyanamide
Cloning, Molecular
Sequence Homology, Amino Acid
Alcohol Dehydrogenase
Isoenzymes
Cytochromes c1
Hevea
Glucuronic Acid
Hydrogen-Ion Concentration
Oxidation-Reduction
Bacteroides
Flavobacterium
Adenylosuccinate Lyase
Streptococcus anginosus
Molecular Structure
NAD
Pseudomonas
Escherichia coli
Sequence Alignment
Glycosaminoglycans
Carbon-Nitrogen Lyases
Proteus vulgaris
Carbon-Carbon Lyases
Uronic Acids
Chondroitin Sulfates
Electrophoresis, Polyacrylamide Gel
Alkenes
Crystallography, X-Ray
Chromatography, High Pressure Liquid
Sulfonium Compounds
Sjogren-Larsson Syndrome
DNA-(Apurinic or Apyrimidinic Site) Lyase
Base Sequence
NADP
Carbohydrate Sequence
Dermatan Sulfate
Chemistry, Organic
Biocatalysis
Liver
Hydrogenation
Catalytic Domain
Fungi
Models, Molecular
Binding Sites
Chromatography
Enzyme Stability
N-Glycosyl Hydrolases
Chromatography, Gel
Phosphoramide Mustards
Organic Chemistry Phenomena
Fatty Alcohols
Temperature
DNA Glycosylases
Coenzymes
Sequence Analysis, DNA
Chromatography, Ion Exchange
Bacillus
Protein Conformation
Lipid Peroxidation
Intramolecular Lyases
Heparitin Sulfate
Molybdenum
Cyclization
Tungsten
Plants
Alkanes
Flushing
Protein Binding
Silanes
Mutation
Ethanol
Plasmalogens
Oligosaccharides
Gene Expression Regulation, Bacterial
Gas Chromatography-Mass Spectrometry
Xanthine Oxidase
Gene Expression Regulation, Enzymologic
Hydrazones
Xanthine Dehydrogenase
Alkynes
Multigene Family
Vibrio
Carboxylic Acids
Magnetic Resonance Spectroscopy
Amines
Mutagenesis, Site-Directed
Organic Chemistry Processes
Boranes
Volatilization
Cell Wall
Crystallization
Phosphorus-Oxygen Lyases
Combinatorial Chemistry Techniques
Lewis Acids
Amination
Lignin
Pyruvaldehyde
Benzyl Alcohols
Mitochondria, Liver
Mass Spectrometry
Waxes
Glutaral
Formaldehyde
Schiff Bases
Retinaldehyde
Biotransformation
Identification and characterization of a DeoR-specific operator sequence essential for induction of dra-nupC-pdp operon expression in Bacillus subtilis. (1/518)
The deoR gene located just upstream the dra-nupC-pdp operon of Bacillus subtilis encodes the DeoR repressor protein that negatively regulates the expression of the operon at the level of transcription. The control region upstream of the operon was mapped by the use of transcriptional lacZ fusions. It was shown that all of the cis-acting elements, which were necessary for full DeoR regulation of the operon, were included in a 141-bp sequence just upstream of dra. The increased copy number of this control region resulted in titration of the DeoR molecules of the cell. By using mutagenic PCR and site-directed mutagenesis techniques, a palindromic sequence located from position -60 to position -43 relative to the transcription start point was identified as a part of the operator site for the binding of DeoR. Furthermore, it was shown that a direct repeat of five nucleotides, which was identical to the 3' half of the palindrome and was located between the -10 and -35 regions of the dra promoter, might function as a half binding site involved in cooperative binding of DeoR to the regulatory region. Binding of DeoR protein to the operator DNA was confirmed by a gel electrophoresis mobility shift assay. Moreover, deoxyribose-5-phosphate was shown to be a likely candidate for the true inducer of the dra-nupC-pdp expression. (+info)Formation of lipoxygenase-pathway-derived aldehydes in barley leaves upon methyl jasmonate treatment. (2/518)
In barley leaves, the application of jasmonates leads to dramatic alterations of gene expression. Among the up-regulated gene products lipoxygenases occur abundantly. Here, at least four of them were identified as 13-lipoxygenases exhibiting acidic pH optima between pH 5.0 and 6.5. (13S,9Z,11E,15Z)-13-hydroxy-9,11,15-octadecatrienoic acid was found to be the main endogenous lipoxygenase-derived polyenoic fatty acid derivative indicating 13-lipoxygenase activity in vivo. Moreover, upon methyl jasmonate treatment > 78% of the fatty acid hydroperoxides are metabolized by hydroperoxide lyase activity resulting in the endogenous occurrence of volatile aldehydes. (2E)-4-Hydroxy-2-hexenal, hexanal and (3Z)- plus (2E)-hexenal were identified as 2,4-dinitro-phenylhydrazones using HPLC and identification was confirmed by GC/MS analysis. This is the first proof that (2E)-4-hydroxy-2-hexenal is formed in plants under physiological conditions. Quantification of (2E)-4-hydroxy-2-hexenal, hexanal and hexenals upon methyl jasmonate treatment of barley leaf segments revealed that hexenals were the major aldehydes peaking at 24 h after methyl jasmonate treatment. Their endogenous content increased from 1.6 nmol.g-1 fresh weight to 45 nmol.g-1 fresh weight in methyl-jasmonate-treated leaf segments, whereas (2E)-4-hydroxy-2-hexenal, peaking at 48 h of methyl jasmonate treatment increased from 9 to 15 nmol.g-1 fresh weight. Similar to the hexenals, hexanal reached its maximal amount 24 h after methyl jasmonate treatment, but increased from 0.6 to 3.0 nmol.g-1 fresh weight. In addition to the classical leaf aldehydes, (2E)-4-hydroxy-2-hexenal was detected, thereby raising the question of whether it functions in the degradation of chloroplast membrane constituents, which takes place after methyl jasmonate treatment. (+info)Molecular analysis of (R)-(+)-mandelonitrile lyase microheterogeneity in black cherry. (3/518)
The flavoprotein (R)-(+)-mandelonitrile lyase (MDL; EC 4.1.2.10), which plays a key role in cyanogenesis in rosaceous stone fruits, occurs in black cherry (Prunus serotina Ehrh.) homogenates as several closely related isoforms. Biochemical and molecular biological methods were used to investigate MDL microheterogeneity and function in this species. Three novel MDL cDNAs of high sequence identity (designated MDL2, MDL4, and MDL5) were isolated. Like MDL1 and MDL3 cDNAs (Z. Hu, J.E. Poulton [1997] Plant Physiol 115: 1359-1369), they had open reading frames that predicted a flavin adenine dinucleotide-binding site, multiple N-glycosylation sites, and an N-terminal signal sequence. The N terminus of an MDL isoform purified from seedlings matched the derived amino acid sequence of the MDL4 cDNA. Genomic sequences corresponding to the MDL1, MDL2, and MDL4 cDNAs were obtained by polymerase chain reaction amplification of genomic DNA. Like the previously reported mdl3 gene, these genes are interrupted at identical positions by three short, conserved introns. Given their overall similarity, we conclude that the genes mdl1, mdl2, mdl3, mdl4, and mdl5 are derived from a common ancestral gene and constitute members of a gene family. Genomic Southern-blot analysis showed that this family has approximately eight members. Northern-blot analysis using gene-specific probes revealed differential expression of the genes mdl1, mdl2, mdl3, mdl4, and mdl5. (+info)Study of the (S)-hydroxynitrile lyase from Hevea brasiliensis: mechanistic implications. (4/518)
Investigations of the (S)-selective hydroxynitrile lyase from Hevea brasiliensis were performed by electrospray mass spectroscopy, (1)H-NMR and with an enzyme activity assay. For the trans-cyanohydrin reaction (transcyanation) a two step reaction could be established. The results furthermore indicate a fast deactivation of the enzyme at low pH and a strong substrate dependence of its stability. They rule out an enzyme-HCN complex or a covalently bound carbonyl compound. Therefore the earlier postulated reaction intermediate as well as the proposed action of the catalytic triad have to be reevaluated. The calculated molecular mass could be confirmed by mass spectroscopy. (+info)Heterologous expression, purification, reconstitution and kinetic analysis of an extended type II polyketide synthase. (5/518)
BACKGROUND: Polyketide synthases (PKSs) are bacterial multienzyme systems that synthesize a broad range of natural products. The 'minimal' PKS consists of a ketosynthase, a chain length factor, an acyl carrier protein and a malonyl transferase. Auxiliary components (ketoreductases, aromatases and cyclases are involved in controlling the oxidation level and cyclization of the nascent polyketide chain. We describe the heterologous expression and reconstitution of several auxiliary PKS components including the actinorhodin ketoreductase (act KR), the griseusin aromatase/cyclase (gris ARO/CYC), and the tetracenomycin aromatase/cyclase (tcm ARO/CYC). RESULTS: The polyketide products of reconstituted act and tcm PKSs were identical to those identified in previous in vivo studies. Although stable protein-protein interactions were not detected between minimal and auxiliary PKS components, kinetic analysis revealed that the extended PKS comprised of the act minimal PKS, the act KR and the gris ARO/CYC had a higher turnover number than the act minimal PKS plus the act KR or the act minimal PKS alone. Adding the tcm ARO/CYC to the tcm minimal PKS also increased the overall rate. CONCLUSIONS: Until recently the principal strategy for functional analysis of PKS subunits was through heterologous expression of recombinant PKSs in Streptomyces. Our results corroborate the implicit assumption that the product isolated from whole-cell systems is the dominant product of the PKS. They also suggest that an intermediate is channeled between the various subunits, and pave the way for more detailed structural and mechanistic analysis of these multienzyme systems. (+info)An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates. (6/518)
Sulfolobus solfataricus is a hyperthermophilic archaeon growing optimally at 80-85 degrees C. It metabolizes glucose via a novel non-phosphorylated Entner-Doudoroff pathway, in which the reversible C(6) to C(3) aldol cleavage is catalysed by 2-keto-3-deoxygluconate aldolase (KDG-aldolase), generating pyruvate and glyceraldehyde. Given the ability of such a hyperstable enzyme to catalyse carbon-carbon-bond synthesis with non-phosphorylated metabolites, we report here the cloning and sequencing of the S. solfataricus gene encoding KDG-aldolase, and its expression in Escherichia coli to give fully active enzyme. The recombinant enzyme was purified in a simple two-step procedure, and shown to possess kinetic properties indistinguishable from the enzyme purified from S. solfataricus cells. The KDG-aldolase is a thermostable tetrameric protein with a half-life at 100 degrees C of 2.5 h, and is equally active with both d- and l-glyceraldehyde. It exhibits sequence similarity to the N-acetylneuraminate lyase superfamily of Schiff-base-dependent aldolases, dehydratases and decarboxylases, and evidence is presented for a similar catalytic mechanism for the archaeal enzyme by substrate-dependent inactivation by reduction with NaBH(4). (+info)Three-dimensional structures of enzyme-substrate complexes of the hydroxynitrile lyase from Hevea brasiliensis. (7/518)
The 3D structures of complexes between the hydroxynitrile lyase from Hevea brasiliensis (Hb-HNL) and several substrate and/or inhibitor molecules, including trichloracetaldehyde, hexafluoracetone, acetone, and rhodanide, were determined by X-ray crystallography. The complex with trichloracetaldehyde showed a covalent linkage between the protein and the inhibitor, which had apparently resulted from nucleophilic attack of the catalytic Ser80-Ogamma. All other complexes showed the substrate or inhibitor molecule merely hydrogen bonded to the protein. In addition, the native crystal structure of Hb-HNL was redetermined at cryo-temperature and at room temperature, eliminating previous uncertainties concerning residual electron density within the active site, and leading to the observation of two conserved water molecules. One of them was found to be conserved in all complex structures and appears to have mainly structural significance. The other water molecule is conserved in all structures except for the complex with rhodanide; it is hydrogen bonded to the imidazole of the catalytic His235 and appears to affect the Hb-HNL catalyzed reaction. The observed 3D structural data suggest implications for the enzyme mechanism. It appears that the enzyme-catalyzed cyanohydrin formation is unlikely to proceed via a hemiacetal or hemiketal intermediate covalently attached to the enzyme, despite the observation of such an intermediate for the complex with trichloracetaldehyde. Instead, the data are consistent with a mechanism where the incoming substrate is activated by hydrogen bonding with its carbonyl oxygen to the Ser80 and Thr11 hydroxy groups. A hydrogen cyanide molecule subsequently replaces a water molecule and is deprotonated presumably by the His235 base. Deprotonation is facilitated by the proximity of the positive charge of the Lys236 side chain. (+info)Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression. (8/518)
The ribulose monophosphate (RuMP) pathway is one of the metabolic pathways for the synthesis of compounds containing carbon-carbon bonds from one-carbon units and is found in many methane- and methanol-utilizing bacteria, which are known as methylotrophs. The characteristic enzymes of this pathway are 3-hexulose-6-phosphate synthase (HPS) and 6-phospho-3-hexuloisomerase (PHI), neither of which was thought to exist outside methylotrophs. However, the presumed yckG gene product (YckG) of Bacillus subtilis shows a primary structure similar to that of methylotroph HPS (F. Kunst et al., Nature 390:249-256, 1997). We have also investigated the sequence similarity between the yckF gene product (YckF) and methylotroph PHI (Y. Sakai, R. Mitsui, Y. Katayama, H. Yanase, and N. Kato, FEMS Microbiol. Lett. 176:125-130, 1999) and found that the yckG and yckF genes of B. subtilis express enzymatic activities of HPS and PHI, respectively. Both of these activities were concomitantly induced in B. subtilis by formaldehyde, with induction showing dependence on the yckH gene, but were not induced by methanol, formate, or methylamine. Disruption of either gene caused moderate sensitivity to formaldehyde, suggesting that these enzymes may act as a detoxification system for formaldehyde in B. subtilis. In conclusion, we found an active yckG (for HPS)-yckF (for PHI) gene structure (now named hxlA-hxlB) in a nonmethylotroph, B. subtilis, which inherently preserves the RuMP pathway. (+info)* Intellectual disability: Individuals with Sjogren-Larsson syndrome typically have mild to moderate intellectual disability, which can range from mild cognitive impairment to more severe developmental delays.
* Seizures: Seizures are a common feature of Sjogren-Larsson syndrome, and they can be difficult to control with medication.
* Physical abnormalities: Individuals with Sjogren-Larsson syndrome may have distinctive physical features, such as short stature, thinning of the hair on the scalp, and thin, brittle skin. They may also have joint deformities, such as clubfoot or scoliosis.
* Vision problems: Sjogren-Larsson syndrome can cause vision problems, including nearsightedness, farsightedness, and astigmatism.
* Hearing loss: Some individuals with Sjogren-Larsson syndrome may experience hearing loss or auditory processing disorders.
There is no cure for Sjogren-Larsson syndrome, but various treatments can help manage the symptoms. These may include medications to control seizures, physical therapy to improve joint mobility and strength, and occupational therapy to develop daily living skills. In addition, speech and language therapy may be helpful for individuals with hearing loss or communication difficulties.
Early diagnosis of Sjogren-Larsson syndrome is important to ensure that children receive appropriate interventions and support as early as possible. Diagnosis typically involves a combination of clinical evaluation, genetic testing, and imaging studies, such as MRI or CT scans. Genetic counseling can also be helpful for families who have a history of the condition.
Overall, Sjogren-Larsson syndrome is a rare and complex disorder that requires careful management and support. With appropriate interventions and resources, individuals with this condition can lead fulfilling lives.
Flushing can also be a side effect of certain medications, such as beta-blockers, aspirin, and some antidepressants. In addition, flushing can be a sign of an underlying condition that affects blood flow or blood vessels, such as Raynaud's disease or lupus.
Treatment for flushing will depend on the underlying cause. For example, if flushing is caused by an allergic reaction, medications such as antihistamines may be prescribed. If the flushing is caused by a medical condition, treatment will focus on managing that condition. In some cases, lifestyle changes such as avoiding triggers, wearing protective clothing, and using cool compresses can help reduce flushing.
It is important to seek medical attention if flushing is severe, persistent, or accompanied by other symptoms such as fever, chest pain, or difficulty breathing. Your healthcare provider can diagnose the underlying cause of flushing and recommend appropriate treatment.
4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase
Hydroxynitrilase
Ketotetrose-phosphate aldolase
Phosphoketolase
17-alpha-hydroxyprogesterone aldolase
Vanillin synthase
Lactoylglutathione lyase
6-Nonenal
Ethanolamine-phosphate phospho-lyase
DNA glycosylase
Base excision repair
Hydroxymandelonitrile lyase
Fucosterol-epoxide lyase
Indole-3-glycerol-phosphate lyase
Lyase
Mandelonitrile lyase
Threonine aldolase
2-dehydro-3-deoxyglucarate aldolase
Tagatose-bisphosphate aldolase
Rhamnulose-1-phosphate aldolase
Propioin synthase
Fructose-6-phosphate phosphoketolase
Trimethylamine-oxide aldolase
Benzoin aldolase
Lactate aldolase
2-Dehydro-3-deoxy-phosphogluconate aldolase
Phenylserine aldolase
List of MeSH codes (D08)
Dimethylaniline-N-oxide aldolase
Sphinganine-1-phosphate aldolase
Enzyme inhibitor
Angelicin
Olfactory receptor
Malonyl-CoA decarboxylase
Strictosidine synthase
Hexenuronic acid
Glyoxylic acid
Glycolysis
Mandelonitrile
Rancidification
Hemithioacetal
Pisatin
Green leaf volatiles
Protein moonlighting
Henry reaction
1-Aminocyclopropane-1-carboxylate synthase
Vitamin B6
Methylglyoxal synthase
Eugenol
Trans,cis-2,6-Nonadienal
Amino acid
S)-hydroxynitrile lyase
Pyridoxal phosphate
Sphingosine 1-phosphate lyase deficiency causes Charcot-Marie-Tooth neuropathy - PubMed
Publication Detail
MeSH Browser
DeCS
MeSH Browser
Adult Refsum Disease - GeneReviews® - NCBI Bookshelf
Aldehydes. Medical search
LOC Os09g26360.1 details
CRO38139 details
eDGAR: SHMT1 gene page
EOD41084 details
Anti-Hipertensivos/química
NDF-RT Code NDF-RT Name
Biosynthesis of beta-phenethyl alcohol in Candida guilliermondii
GLO1
- Early...
MedlinePlus: Genetic Conditions: C
Research Materials | Technology Transfer
MESH TREE NUMBER CHANGES - 2004 MeSH
Osong Public Health and Research Perspectives
TERM
mediaTUM - Media and Publication Server
Mouse ALDH9A1(Aldehyde Dehydrogenase 9 Family, Member A1) ELISA Kit - World Care Council
Search Results | ASHS
Biomarkers Search
Biosynthesis and Regulation of Antioxidant Flavonolignans in Milk Thistle | IntechOpen
MedlinePlus: Genes
Molecules | Free Full-Text | Genetically Encodable Scaffolds for Optimizing Enzyme Function
Insights into grapevine defense response against drought as revealed by biochemical, physiological and RNA-Seq analysis |...
Hydroperoxide lyase2
- Finally, volatile C6 or C9 aldehydes and 9- or 12-oxoacids are produced with a hydroperoxide lyase. (bvsalud.org)
- In contrast, hydroperoxide lyase (HPL) and Cm-AAT2 and Cm-AAT3 seemed to be independent of ETH modulation. (ashs.org)
Conjugate1
- Screening of β-lyases from other sources, e.g. plants in which thiols play important sensory roles, revealed cysteine conjugate β-lyase activities in passion fruits and in the leaves of blackcurrant and box tree. (tum.de)
Volatiles1
- Green leaf volatiles (GLVs), including short chain volatile aldehydes, are widely used in the flavor and food industries because of their fresh aroma. (bvsalud.org)
Molecules1
- A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules (ALDEHYDES or KETONES). (bvsalud.org)
Structural1
- Structural effects on the activities of C-S β-lyases were investigated by employing synthesized analogues as substrates. (tum.de)
Sphingosine phosphate lyase1
- sphingosine phosphate lyase (Sgpl1), and paraoxonase 1 (Pon1). (nih.gov)
Sgpl11
- Recently recessive mutations in sphingosine-1-phosphate lyase (SGPL1) have been published as a cause of syndromic congenital nephrotic syndrome with adrenal insufficiency. (nih.gov)
Fatty3
- The cleavage of sphingoid base phosphates by sphingosine-1-phosphate (S1P) lyase to produce phosphoethanolamine and a fatty aldehyde is the final degradative step in the sphingolipid metabolic pathway. (nih.gov)
- There was evidence tiiat oxidative changes in polyunsaturated fatty acids in debris led to water-soluble toxic aldehydes tiiat were detectable in the viti:eous and toxic to lens ceUs and membranes. (nih.gov)
- 17. Identification of fatty aldehyde dehydrogenase in the breakdown of phytol to phytanic acid. (nih.gov)
Produce1
- A molecule containing a hydroxyl group and a carbonyl group is cleaved at a C-C bond to produce two smaller molecules ( ALDEHYDES or KETONES ). (nih.gov)