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Its defining modification is a trans -3-hexenoyl group attached to the N-terminal tyrosine, a chemical change designed to protect the peptide from rapid cleavage by dipeptidyl peptidase-4 (DPP-4), the enzyme that quickly inactivates native GHRH
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[1] [2] [3] [4] Bacterial GSTs of known function often have a specific, growth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs
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