Protein Family Models

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)

Date:

2024-10-16

L-serine ammonia-lyase, iron-sulfur-dependent, subunit beta is part of the enzyme complex that catalyzes the deamination of serine to form pyruvate

Date:

2020-10-28

This enzyme is also called serine deaminase. L-serine dehydratase converts serine into pyruvate in the gluconeogenesis pathway from serine. This model describes the alpha chain of an iron-sulfur-dependent L-serine dehydratase, found in Bacillus subtilis. A fairly deep split in a UPGMA tree separates members of this family of alpha chains from the homologous region of single chain forms such as found in Escherichia coli. This family of enzymes is not homologous to the pyridoxal phosphate-dependent threonine deaminases and eukaryotic serine deaminases.

Gene:

sdaAA

Date:

2021-04-27