Thiol groups of soybean callus succinyl CoA synthetase
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چکیده
منابع مشابه
The Crystal Structure of Succinyl-CoA Synthetase
The x-ray crystal structure of succinyl-CoA synthetase (SCS) from Escherichia coli has been determined by the method of mu!tiple isomorphous replacement to a resolution of 2.5 A. Crystals of SCS are tetragonal with a space group of P4,22 oand unit cell dimensions of a = b = 98.47 A and c = 400.6 A. One molecule of SCS (142 kDa) is contained in the asymmetric unit. The current model has been ref...
متن کاملIdentification of the kinetic mechanism of succinyl-CoA synthetase
The kinetic mechanism of SCS [succinyl-CoA (coenzyme A) synthetase], which participates in the TCA (tricarboxylic acid) cycle, ketone body metabolism and haem biosynthesis, has not been fully characterized. Namely, a representative catalytic mechanism and associated kinetic parameters that can explain data on the enzyme-catalysed reaction kinetics have not been established. To determine an accu...
متن کاملSuccinyl-CoA Synthetase: New Antigen Candidate of Bartonella bacilliformis
BACKGROUND Bartonella bacilliformis is the causative agent of Carrion's disease, a neglected illness with mortality rates of 40-85% in the absence of treatment. The lack of a diagnostic technique to overcome misdiagnosis and treat asymptomatic carriers is of note. This study aimed to identify new B. bacilliformis antigenic candidates that could lead to a new diagnostic tool able to be implement...
متن کاملLocalization and nucleotide specificity of Blastocystis succinyl-CoA synthetase
The anaerobic lifestyle of the intestinal parasite Blastocystis raises questions about the biochemistry and function of its mitochondria-like organelles. We have characterized the Blastocystis succinyl-CoA synthetase (SCS), a tricarboxylic acid cycle enzyme that conserves energy by substrate-level phosphorylation. We show that SCS localizes to the enigmatic Blastocystis organelles, indicating t...
متن کاملNovel Reaction of Succinyl Coenzyme A (Succinyl-CoA) Synthetase: Activation of 3-Sulfinopropionate to 3-Sulfinopropionyl-CoA in Advenella mimigardefordensis Strain DPN7 during Degradation of 3,3 -Dithiodipropionic Acid †
The sucCD gene of Advenella mimigardefordensis strain DPN7 encodes a succinyl coenzyme A (succinyl-CoA) synthetase homologue (EC 6.2.1.4 or EC 6.2.1.5) that recognizes, in addition to succinate, the structural analogues 3-sulfinopropionate (3SP) and itaconate as substrates. Accumulation of 3SP during 3,3 -dithiodipropionic acid (DTDP) degradation was observed in Tn5::mob-induced mutants of A. m...
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ژورنال
عنوان ژورنال: International Journal of Biochemistry
سال: 1974
ISSN: 0020-711X
DOI: 10.1016/0020-711x(74)90143-8