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L-serine ammonia-lyase, iron-sulfur-dependent, subunit alpha
L-serine dehydratase (EC:4.2.1.13) is a found as a heterodimer of alpha and beta chain or as a fusion of the two chains in a single protein. This enzyme catalyses the deamination of serine to form pyruvate. This enzyme is part of the gluconeogenesis pathway. Members included in this entry adopt and all-helical structure [1]. [1]. 25380533. Structure of L-serine dehydratase from Legionella pneumophila:. novel use of the C-terminal cysteine as an intrinsic competitive. inhibitor.. Thoden JB, Holden HM, Grant GA;. Biochemistry. 2014;53:7615-7624. (from Pfam)
serine dehydratase subunit alpha family protein
serine dehydratase subunit alpha family protein such as L-cysteine desulfidase, which catalyzes the cleavage of L-cysteine to form 2-aminoprop-2-enoate and sulfide
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