Category:Complex:alpha subunit complex: Difference between revisions
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==About== | ==About== | ||
'''Description''' (originally from EcoCyc<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>) α subunit complex | '''Description''' (originally from EcoCyc<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>) α subunit complex | ||
'''Comments''' (originally from EcoCyc<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>) The alpha subunit plays an essential role in the catalytic mechanism of the | |||
enzyme and in the binding and coupling between the F-1 and F-O complexes. The | |||
alpha-subunit also contains an adenine-specific binding site which is | |||
noncatalytic, nonregulatory and not essential for enzyme assembly in vitro. Its | |||
function has not yet been determined. The alpha subunit complex is a homotrimer. | |||
<ref name='PMID:2903146'/> | |||
Revision as of 08:09, 2 August 2007
About
Description (originally from EcoCyc[1][2]) α subunit complex
Comments (originally from EcoCyc[1][2]) The alpha subunit plays an essential role in the catalytic mechanism of the enzyme and in the binding and coupling between the F-1 and F-O complexes. The alpha-subunit also contains an adenine-specific binding site which is noncatalytic, nonregulatory and not essential for enzyme assembly in vitro. Its function has not yet been determined. The alpha subunit complex is a homotrimer. [3]
References
- ↑ 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Rao, R et al. (1988) Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase. J Biol Chem 263 15957-63 PubMed
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