Formation of -cyanoalanine by O-acetylserine sulfhydrylase.

نویسندگان

  • P A Castric
  • E E Conn
چکیده

Cell-free extracts of Bacillus megaterium form beta-cyanoalanine (beta-CNA)-(14)C from Na(14)CN and l-cysteine, O-acetyl-l-serine or, to a lesser extent, l-serine. However, the presence of cyanide in the growth medium does not increase the capacity of cell extracts to catalyze the formation of beta-CNA from cysteine and cyanide. The formation of beta-CNA is readily detected in extracts of cells grown in synthetic media with sulfate or l-djenkolic acid as sulfur sources; such cells also exhibit an increased ability to form cysteine when compared with cells grown on cysteine as the sulfur source. beta-CNA formation could not be detected in extracts of cells grown on cysteine as the sulfur source. A 40-fold purification of the O-acetyl-serine sulfhydrylase resulted in the co-purification of the beta-CNA-forming activity. The sulfhydrylase and the beta-CNA-forming activity co-chromatographed on diethyl-aminoethyl cellulose and Sephadex G-100.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Isozyme-Specific Ligands for O-acetylserine sulfhydrylase, a Novel Antibiotic Target

The last step of cysteine biosynthesis in bacteria and plants is catalyzed by O-acetylserine sulfhydrylase. In bacteria, two isozymes, O-acetylserine sulfhydrylase-A and O-acetylserine sulfhydrylase-B, have been identified that share similar binding sites, although the respective specific functions are still debated. O-acetylserine sulfhydrylase plays a key role in the adaptation of bacteria to...

متن کامل

The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase.

The biosynthesis of cysteine in bacteria and plants is carried out by a two-step pathway, catalyzed by serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS in complex with a C-terminal peptide of SAT...

متن کامل

Pleiotrophy in a cysteine-requiring mutant of Samonella typhimurium resulting from altered protein-protein interaction.

The bifunctional protein complex, cysteine synthetase, in Salmonella tyPhimurium is composed of the enzymes serine transacetylase and 0-acetylserine sulfhydrylase. A point mutation (BBl) in the structural gene for serine transacetylase results in diminished catalytic activity of both components of the complex. Enzyme inactivation studies using either specific 0-acetylserine sulfhydrylase antise...

متن کامل

Cysteine synthase (O-acetylserine (thiol) lyase) substrate specificities classify the mitochondrial isoform as a cyanoalanine synthase.

A cyanoalanine synthase and two isoforms (A, cytosolic and B, chloroplastic) of cysteine synthase (O:-acetylserine (thiol) lyase) were isolated from spinach. N-terminal amino acid sequence analysis of the cyanoalanine synthase gave 100% homology for the determined 12 residues with a published sequence for the mitochondrial cysteine synthase isoform. All three enzymes catalysed both the cysteine...

متن کامل

The structural gene for O-acetylserine sulfhydrylase A in Salmonella typhimurium. Identity with the trzA locus.

Mutants of Salmonella typhimurium, resistant to 1,2,4triazole and mapping in the trzA and trzB loci, have been found to have low to virtually absent levels of 0-acetylserine sulfhydrylase activity while remaining prototrophic for cysteine. Kinetic, chemical, and immunochemical studies of the highly purified enzymes from two trzA mutants prove that both strains bear mutant alleles for 0-acetylse...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of bacteriology

دوره 108 1  شماره 

صفحات  -

تاریخ انتشار 1971