Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Structure of human cystathionine β‐synthase: a unique pyridoxal 5′‐phosphate‐dependent heme protein
The X‐ray crystal structure of a truncated form of CBS, a unique heme‐ containing enzyme that catalyzes a pyridoxal 5′‐phosphate‐dependent condensation of serine and homocysteine to give cystathionine, is presented.
Expression of human cystathionine beta-synthase in Escherichia coli: purification and characterization.
Human CBS cDNA is cloned in tandem with the beta-galactosidase sequence of the fusion vector, pAX5-, then the fusion protein is expressed in transformed Escherichia coli cells, marking the first time this enzyme has been isolated in sufficient quantities for biophysical and biochemical investigation.
Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM.
It is proposed that the SAM-induced stabilization may play a key role in modulating steady-state levels of WT and mutant CBS in vivo, valuable for understanding ligand effects on proteins with a complex architecture and their role in human genetic diseases and for the development of novel pharmacological strategies.
Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.
- E. Spicer, R. Horton, +7 authors W. Konigsberg
- Biology, MedicineProceedings of the National Academy of Sciences…
- 1 August 1987
The amino acid sequence deduced from the nucleotide sequence of the cDNAs indicates that tissue factor is synthesized as a higher molecular weight precursor with a leader sequence of 32 amino acids, while the mature protein is a single polypeptide chain composed of 263 residues.
Propionic acidemia: clinical course and outcome in 55 pediatric and adolescent patients
- S. Grünert, S. Müllerleile, +27 authors J. Sass
- MedicineOrphanet Journal of Rare Diseases
- 10 January 2013
The data show that the outcome of propionic acidemia is still unfavourable, in spite of improved clinical management, and that Impairment of neurocognitive development is of special concern.
Cystathionine beta-synthase mutations in homocystinuria.
The major cause of homocystinuria is mutation of the gene encoding the enzyme cystathionine beta-synthase (CBS), and mutations due to deaminations of methylcytosines represent 53% of all point substitutions in the coding region of the CBS gene.
Transsulfuration depends on heme in addition to pyridoxal 5'-phosphate. Cystathionine beta-synthase is a heme protein.
- V. Kéry, G. Bukovska, J. Kraus
- Medicine, ChemistryThe Journal of biological chemistry
- 14 October 1994
It is suggested that heme is functionally incorporated into CBS only during protein folding, and the first instance of an enzyme that depends upon both heme and PLP for its function is described.
Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences.
- V. Kéry, L. Poneleit, J. Kraus
- Chemistry, MedicineArchives of biochemistry and biophysics
- 15 July 1998
It is found that the COOH-terminal region, residues 414-551, is essential for maintaining the tetrameric structure and AdoMet activation of the enzyme.
The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms.
The molecular cloning and the complete nucleotide sequence of the human CBS gene is described and the identification of two alternatively used promoter regions that are GC rich (approximately 80%) and contain numerous putative binding sites for Sp1, Ap 1, Ap2, and c-myb, but lack the classical TATA box.
Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient.
- L. Kluijtmans, G. Boers, +5 authors H. Blom
- Biology, MedicineThe Journal of clinical investigation
- 15 July 1996
The presence of a homozygous G1330A mutation in the CBS cDNA indicates the importance of S-adenosylmethionine regulation of the transsulfuration pathway in homocysteine homeostasis in humans and suggests that this D444N mutation interferes in S- adenosyl methionines regulation of CBS.