MetC Protein, E.coli (E. coli, His)

MetC protein is a multifunctional enzyme that catalyzes the cleavage of cystathionine to homocysteine, pyruvate, and ammonia, which is essential for methionine biosynthesis. It also acts as a cysteine desulfurase, converting cysteine into sulfide. MetC Protein, E.coli (E. coli, His) is the recombinant E. coli-derived MetC protein, expressed by E. coli , with N-His labeled tag. The total length of MetC Protein, E.coli (E. coli, His) is 392 a.a., with molecular weight of ~46.8 kDa.

The MetC protein serves as a multifunctional enzyme with a primary role in catalyzing the cleavage of cystathionine to homocysteine, pyruvate, and ammonia, a critical step in methionine biosynthesis. Beyond its primary function, MetC demonstrates cysteine desulfhydrase activity, converting cysteine into sulfide. Moreover, under specific growth conditions, the protein exhibits noteworthy coactivity as an alanine racemase. This versatile enzymatic repertoire highlights MetC's involvement in diverse metabolic pathways, showcasing its capacity to contribute to the intricate regulation of amino acid metabolism and biosynthetic processes.

E.coli

E. coli

N-His

P06721 (1M-392A)

946240  [NCBI]

MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLNNEELANYLDNFSLFSMAYSWGGYESLILANQPEHIAAIRPQGEIDFSGTLIRLHIGLEDVDDLIADLDAGFA

Approximately 46.8 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.