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Literature summary for 2.3.1.86 extracted from

  • Singh, K.; Graf, B.; Linden, A.; Sautner, V.; Urlaub, H.; Tittmann, K.; Stark, H.; Chari, A.
    Discovery of a regulatory subunit of the yeast fatty acid synthase (2020), Cell, 180, 1130-1143 .
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
a gamma subunit of the 2.6 megadalton FAS16-FAS26 stabilizes a rotated FAS conformation and rearranges ACP domains from equatorial to axial positions. The gamma subunit spans the length of the FAS inner cavity, impeding reductase activities of FAS, regulating NADPH turnover by kinetic hysteresis at the ketoreductase, and suppressing off-pathway reactions at the enoylreductase. The gamma subunit delineates the functional compartment within FAS Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P07149 and P19097 and Q12513 P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2, Q12513 i.e. gamma-subunit Tma17
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Saccharomyces cerevisiae ATCC 204508 P07149 and P19097 and Q12513 P07149 i.e.subunit FAS1, P19097 i.e. subunit FAS2, Q12513 i.e. gamma-subunit Tma17
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General Information

General Information Comment Organism
physiological function translation machinery-associated protein Tma17 copurifies with FAS complex. 6 copies of Tma17p can simultaneously bind to one FAS molecule, binding follows a positive cooperativity. Tma17 acts as FAS gamma subunit regulating the activity in response to the abundance of cosubstrate NADPH Saccharomyces cerevisiae