Titlebook: Biochemistry of Vitamin B6; Proceedings of the 7 Timo K. Korpela,Philipp Christen Conference proceedings 1987 Birkhäuser Verlag Basel 1987

Extraneous

书目名称Biochemistry of Vitamin B6影响因子(影响力)




书目名称Biochemistry of Vitamin B6影响因子(影响力)学科排名




书目名称Biochemistry of Vitamin B6网络公开度




书目名称Biochemistry of Vitamin B6网络公开度学科排名




书目名称Biochemistry of Vitamin B6被引频次




书目名称Biochemistry of Vitamin B6被引频次学科排名




书目名称Biochemistry of Vitamin B6年度引用




书目名称Biochemistry of Vitamin B6年度引用学科排名




书目名称Biochemistry of Vitamin B6读者反馈




书目名称Biochemistry of Vitamin B6读者反馈学科排名

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LEER

Closing Remarkslä, Dr. Timo Korpela, Dr. Seppo Sarimo and all of those who have helped them to make this a pleasant and productive symposium. Their young helpers in the blue and white shirts have charmed us all. Their efforts, the friendliness of the people of Turku, and the beautiful midsummer nights have combine

STALE

Genes, Biosynthesis, and Intracellular Processing of the Iso-Enzymes of Aspartate Aminotransferasegenes, and are synthesized on free polysomes. The precursor contains a basic NH.-terminal prepiece. The genes of the two homologous isoenzymes possess similarly positioned exon-intron boundaries. The prepiece of mAspAT is encoded by one (or more) separate exon(s). Pre-mAspAT cDNA and mAspAT cDNA hav

客观

Structure-Function Relation of the Presequence of a Precursor to Pig Mitochondrial Aspartate Aminotrithin its presequence were tested. The amino-terminal portion is essential for mitochondrial uptake and processing. The presence of two positively charged residues, Hisl8 and Arg28, may not be requisite for the uptake, but the processing efficiency was reduced by the single amino acid change, Arg28

挣扎

D-Amino Acid Aminotransferase from a Thermophile, , SP. YM-1: Enzymological Properties, Cloning of tbacterium (. sp. YM-1) showed a very high activity of D-amino acid aminotransferase. The enzyme purified to homogeneity from cell extracts of YM-1 has a molecular weight of about 62,000, and is composed of two subunits identical in molecular weight (30,000). The D-amino acid aminotransferase gene wa

利用

iodides

Herbivorous

SEED

Mechanistic Analysis of the Aspartate Aminotransferase Active Site Mutants—Y70F, K258A, and R292Dt Y70 is not an . amino acid for catalysis. Rather, this residue does provide an important functional role in substantially reducing the rate constant for cofactor dissociation from the enzyme. The PMP form of K258A reacts with α-ketoglutarate to give the ketimine as a stable final product. The corr