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Kinetic and structural insights into enzymatic mechanism of succinic semialdehyde dehydrogenase from Cyanothece sp. ATCC51142

Fig 5

Amino acid sequence alignment of succinic semialdehyde dehydrogenases from different sources.

SSADH sequences retrieved from the National Center for Biotechnology Information (NCBI): cce4228 protein from Cyanothece sp. ATCC51142 (ACB53576), all3556 from Anabaena sp. PCC7120 (BAB75255), a2771 from Synechococcus sp. PCC7002 (ACB00745), YneI from Samlonella typhimurium (NP_460484), YneI from E. coli (WP_115463367), GabD from E. coli (NP_417147), GabD from Human (NP_001071), GabD from A. thaliana (NP_178062), YneI from Bacillus subtilis (ARW30050). Triangle indicates residues involved in cofactor preference, and pentagram indicates residues involved in enzyme catalysis.

Fig 5

doi: https://doi.org/10.1371/journal.pone.0239372.g005