(Q28139168)

English

Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein

scientific article (publication date: 26 March 1999)

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scholarly article

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Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein (English)

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Acetoanaerobium sticklandii

object named as

Clostridium sticklandii

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based on heuristic

inferred from title

author name string

U C Kabisch

1

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A Gräntzdörffer

2

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A Schierhorn

3

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K P Rücknagel

4

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J R Andreesen

5

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A Pich

6

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language of work or name

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publication date

26 March 1999

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Journal of Biological Chemistry

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274

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13

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8445-54

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Fast purification of thioredoxin reductases and of thioredoxins with an unusual redox-active centre from anaerobic, amino-acid-utilizing bacteria.

1 reference

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Glycine metabolism in anaerobes

1 reference

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Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis

1 reference

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Purification and characterization of protein PC, a component of glycine reductase from Eubacterium acidaminophilum

1 reference

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Interaction of selenoprotein PA and the thioredoxin system, components of the NADPH-dependent reduction of glycine in Eubacterium acidaminophilum and Clostridium litorale [corrected]

1 reference

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21 January 2018

Components of glycine reductase from Eubacterium acidaminophilum. Cloning, sequencing and identification of the genes for thioredoxin reductase, thioredoxin and selenoprotein PA.

1 reference

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21 January 2018

NADH-dependent reduction of d-proline in Clostridium sticklandii. Reconstitution from three fractions containing NADH dehydrogenase, d-proline reductase, and a third protein factor

1 reference

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Proline reductase: A sensitive fluorometric assay with o-phthalaldehyde

1 reference

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

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A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

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DNA sequencing with chain-terminating inhibitors

1 reference

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Clostridium sticklandii glycine reductase selenoprotein A gene: cloning, sequencing, and expression in Escherichia coli

1 reference

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Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue.

1 reference

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21 January 2018

The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites

1 reference

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Prediction of rho-independent Escherichia coli transcription terminators. A statistical analysis of their RNA stem-loop structures.

1 reference

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Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine

1 reference

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Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing

1 reference

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Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes

1 reference

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Identifiers

10.1074/JBC.274.13.8445

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