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Báo cáo khoa học: Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage Crystal structure and biochemical studies

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:14

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Serine hydroxymethyltransferase (SHMT) fromBacillus stearothermophilus (bsSHMT) is a pyridoxal 5¢-phosphate-dependent enzyme that catalyses the conversion of l-serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. In addition, the enzyme catalyses the tetrahydrofolate-independent cleavage of 3-hydroxy amino acids and transamination.

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Nội dung Text: Báo cáo khoa học: Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and L-allo-Thr cleavage Crystal structure and biochemical studies

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