Enzyme cystathionine1.22Gamma lyaseTranssulfuration pathwayLyaseCysteineHomocysteineProteinsMembraneHumanReceptorFunctionalBindingDomainBasisStepMainHomocystinuriaDeficiencyEnzymeMethylcysteine synthaseMutationsRegulationProteinMutationCofactorGenesLigandsCharacterizationRegulatoryReactionGolgiActivityFunctionalProcessPropertiesStudiesOrder
Enzyme cystathionine3
- The human enzyme cystathionine β-synthase is a tetramer and comprises 551 amino acids with a subunit molecular weight of 61 kDa. (wikipedia.org)
- It is caused by a mutation in the gene encoding the enzyme cystathionine beta-synthase (CBS). (rarediseaseshealthcenter.com)
- We therefore determined the role for the endogenous H 2 S producing enzyme cystathionine-β-synthetase (CBS) in a validated rat model of IBS-like chronic visceral hyperalgesia (CVH). (biomedcentral.com)
1.221
- Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. (wikipedia.org)
Gamma lyase1
- Transsulfuration, catalyzed by CBS, converts homocysteine to cystathionine, which cystathione gamma lyase converts to cysteine. (wikipedia.org)
Transsulfuration pathway1
- It catalyzes the first step of the transsulfuration pathway, from homocysteine to cystathionine: L-serine + L-homocysteine ⇌ {\displaystyle \rightleftharpoons } L-cystathionine + H2O CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). (wikipedia.org)
Lyase1
- Other names in common use include: β-thionase, cysteine synthase, L-serine hydro-lyase (adding homocysteine), methylcysteine synthase, serine sulfhydrase, and serine sulfhydrylase. (wikipedia.org)
Cysteine2
- A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. (cathdb.info)
- Cystathionine β-synthase (CBS) is a key regulator of sulfur amino acid metabolism, taking homocysteine from the methionine cycle to the biosynthesis of cysteine via the trans-sulfuration pathway. (rhea-db.org)
Homocysteine2
- Nucleophilic attack by the thiolate of homocysteine on the aminoacrylate and reprotonation at Cα generate the external aldimine of cystathionine. (wikipedia.org)
- L-serine + L-homocysteine = L-cystathionine + H(2)O. (cathdb.info)
Proteins2
- SCOPe: Structural Classification of Proteins - extended. (berkeley.edu)
- The main structural proteins of CAVEOLAE. (lookformedical.com)
Membrane1
- ATP synthase membrane subunit c locus 3. (gsea-msigdb.org)
Human9
- Structural basis of regulation and oligomerization of human cystathionine beta-synthase, the central enzyme of transsulfuration. (cathdb.info)
- Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM. (illumina.com)
- We have successfully used a DNA.cDNA molecular hybridization assay to directly determine the presence or absence of human beta globin gene sequences in 20 human-mouse somatic cell hybrids, each of which contained a different subset of human chromosomes. (eurekamag.com)
- All human chromosomes were present in one or more cell lines devoid of the human beta globin gene except for 6, 8, 9, 11, and 13. (eurekamag.com)
- Among these latter chromosomes, only chromosome 11 was present in the six hybrid clones that contained the human beta globin gene. (eurekamag.com)
- In fact, chromosome 11 was the only human chromosome that was present in all of the six hybrid clones found to be positive for the human beta globin gene. (eurekamag.com)
- 157-BNPT-4 contained the human beta globin gene while 157-BNPT-1 did not. (eurekamag.com)
- two lines positive for human beta globin gene sequences also contained human gamma globin gene sequences while one line was negative for both beta and gamma gene sequences. (eurekamag.com)
- On the basis of these results, the human beta and gamma globin genes have been assigned to human chromosome 11. (eurekamag.com)
Receptor1
- Although Rhinolophus bats harbor diverse clade 3 sarbecoviruses, the structural determinants of receptor tropism along with the antigenicity of their spike (S) glycoproteins remain uncharacterized. (uw.edu)
Functional2
- Structural and functional characterization of the dimerization region of soluble guanylyl cyclase. (org.gr)
- The elucidation and description of the molecular and structural features of gasotransmitters, their production pathways, signaling mechanisms, cellular and molecular targets, and functional impact in prokaryotic and eukaryotic cells are the focus of this book. (rsc.org)
Binding1
- Rod binding protein, Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [Interproscan]. (ntu.edu.sg)
Domain2
- The C-terminal domain of cystathionine β-synthase regulates its activity via both intrasteric and allosteric effects and is important for maintaining the tetrameric state of the protein. (wikipedia.org)
- CBS from Saccharomyces cerevisiae (yCBS) naturally lacks the heme-containing N-terminal domain, which makes it an ideal model for spectroscopic studies of the enzymological reaction catalyzed and allows structural studies of the basic yCBS catalytic core (yCBS-cc). (rhea-db.org)
Basis1
- Crystal structures of yCBS-cc in complex with enzymatic reaction intermediates have been captured, providing a structural basis for residues involved in catalysis. (rhea-db.org)
Step1
- Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time. (rhea-db.org)
Main1
- The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. (lookformedical.com)
Homocystinuria7
- The molecular basis of cystathionine beta-synthase (CBS) deficiency in UK and US patients with homocystinuria. (medlineplus.gov)
- 6. Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria. (nih.gov)
- 7. Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria. (nih.gov)
- 8. Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): Identification and functional analysis of CBS gene mutations in Homocystinuria patients. (nih.gov)
- 16. Targeting Cystathionine Beta-Synthase Misfolding in Homocystinuria by Small Ligands: State of the Art and Future Directions. (nih.gov)
- 19. Kinetic stability of cystathionine beta-synthase can be modulated by structural analogs of S-adenosylmethionine: Potential approach to pharmacological chaperone therapy for homocystinuria. (nih.gov)
- Patients with homocystinuria due to cystathionine beta-synthase (CBS) deficiency may also have elevated plasma methionine concentrations. (nih.gov)
Deficiency1
- 11. Correction of cystathionine β-synthase deficiency in mice by treatment with proteasome inhibitors. (nih.gov)
Enzyme7
- Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. (wikipedia.org)
- The human enzyme cystathionine β-synthase is a tetramer and comprises 551 amino acids with a subunit molecular weight of 61 kDa. (wikipedia.org)
- The CBS gene provides instructions for making an enzyme called cystathionine beta-synthase. (medlineplus.gov)
- Another enzyme then converts cystathionine to the amino acid cysteine, which is used to build proteins or is broken down and excreted in urine. (medlineplus.gov)
- A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. (cathdb.info)
- Structural basis of regulation and oligomerization of human cystathionine beta-synthase, the central enzyme of transsulfuration. (cathdb.info)
- The enzyme cystathionine gamma-lyase converts the cystathionine into cysteine and alpha-ketobutyrate . (cloudfront.net)
Methylcysteine synthase1
- Methylcysteine synthase was assigned the EC number EC 4.2.1.23 in 1961. (wikipedia.org)
Mutations7
- Most of these mutations change single amino acids in cystathionine beta-synthase. (medlineplus.gov)
- These mutations disrupt the normal function of cystathionine beta-synthase. (medlineplus.gov)
- Cystathionine beta-synthase mutations: effect of mutation topology on folding and activity. (medlineplus.gov)
- Meier M, Oliveriusova J, Kraus JP, Burkhard P. Structural insights into mutations of cystathionine beta-synthase. (medlineplus.gov)
- 12. Characterization of two pathogenic mutations in cystathionine beta-synthase: different intracellular locations for wild-type and mutant proteins. (nih.gov)
- 17. Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. (nih.gov)
- Mutations in mitochondrial DNA encoded subunit of ATP synthase, MT-ATP6, are frequent causes of neurological mitochondrial diseases with a range of phenotypes from Leigh syndrome and NARP to ataxias and neuropathies. (biomed.news)
Regulation2
- Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. (medlineplus.gov)
- 13. Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. (nih.gov)
Protein5
- Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein. (nih.gov)
- Deletion of the regulatory domain in the pyridoxal phosphate-dependent heme protein cystathionine beta-synthase alleviates the defect observed in a catalytic site mutant. (nih.gov)
- The C-terminal domain of cystathionine β-synthase regulates its activity via both intrasteric and allosteric effects and is important for maintaining the tetrameric state of the protein. (wikipedia.org)
- Our structures represent the first example of a CBS domain protein complexed with SAM and/or MTA and might provide a structural basis for understanding the molecular mechanisms regulated by SAM upon binding to the C-terminal domain of human CBS, whose structure remains unknown. (nih.gov)
- However, the mechanism of IDR-mediated protein-protein interactions is poorly understood because of a lack of information on their structural preferences and dynamic properties at atomic resolution. (foxchase.org)
Mutation1
- Accordingly, the MT-ATP6 truncating mutation impaired the assembly of ATP synthase and disrupted cristae morphology, supporting our molecular dynamics simulations that predicted destabilized a/c subunit subcomplex. (biomed.news)
Cofactor2
- The complex, in combination with mutagenesis and kinetic data, provides a structural basis for understanding the mechanism of IMPDH activity and indicates that MPA inhibits IMPDH by acting as a replacement for the nicotinamide portion of the nicotinamide adenine dinucleotide cofactor and a catalytic water molecule. (embl.de)
- Consequently, this review goes beyond the classical role of vitamin B 6 as a cofactor to highlight new structural and regulatory information that further defines how the vitamin is synthesized and controlled in the cell. (mdpi.com)
Genes1
- The discovery of genes responsible for inherited colorectal cancer syndromes has been important in identifying important etiologic pathways such as the beta-catenin/ APC and TGF beta/SMAD pathways. (cdc.gov)
Ligands1
- 2. Restoring assembly and activity of cystathionine β-synthase mutants by ligands and chemical chaperones. (nih.gov)
Characterization2
- 1. Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes. (nih.gov)
- 15. Folding and activity of mutant cystathionine β-synthase depends on the position and nature of the purification tag: characterization of the R266K CBS mutant. (nih.gov)
Regulatory1
- In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function. (umbc.edu)
Reaction2
- Glycine can also be formed from CO 2, NH 4 + , and mTHF in a reaction catalyzed by glycine synthase . (iiab.me)
- Cystathionine beta synthase catalyzes the upper reaction and cystathionine gamma-lyase catalyzes the lower reaction. (iiab.me)
Golgi1
- the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). (nih.gov)
Activity1
- Antifungal activity is via inhibition of 1,3-beta-glucan synthase production of BETA-GLUCANS. (lookformedical.com)
Functional1
- During such development, porcine oocytes undergo the complex of the structural and functional changes, which can result in spontaneous parthenogenetic activation, fragmentation or lysis. (nusl.cz)
Process1
- Inhibition of enzymes catalyzing the synthesis of hydrogen sulfide in the oocytes during the process of aging (cystathionine-gamma-lyase and cystathionine beta-synthase), iniciates earlier onset of oocytes fragmentation. (nusl.cz)
Properties1
- 3. Conformational properties of nine purified cystathionine β-synthase mutants. (nih.gov)
Studies1
- Genome-wide studies of structural variation will likely identify deletions, amplifications, and other copy number variations influencing colorectal cancer risk. (cdc.gov)
Order1
- 03. Sex, age at transplant, order of transplant, and presence of structural liver disease did not significantly impact survival. (clinicforspecialchildren.org)