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Literature summary for 7.1.2.2 extracted from
- Role of short conserved segments of alpha- and beta-subunits that link F1-ATPase catalytic and noncatalytic sites (2010), Biochemistry (Moscow), 75, 81-84.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| alphaF244C | the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme | Bacillus sp. PS3 |
| alphaG351D | mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites | Bacillus sp. PS3 |
| alphaR304C | the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme | Bacillus sp. PS3 |
| alphaS347F | mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites | Bacillus sp. PS3 |
| alphaS373F | mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites | Bacillus sp. PS3 |
| alphaS375F | mutation of a residue of a linking segment involved in transduction of the conformation signal between catalytic and noncatalytic sites | Bacillus sp. PS3 |
| alphaY300C | the mutation causes a change in excess Mg2+-dependent degree of ATPase activity inhibition, and thus a different level of MgADP-induced inactivation of the enzyme | Bacillus sp. PS3 |
| additional information | mutations at the C-terminal part of the gamma-subunit of chloroplast F1 reconstituted with the F1 alpha and beta subunits of the photosynthesizing bacterium affect conformation signal transduction between the catalytic and noncatalytic sites | Rhodospirillum rubrum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast membrane | - |
Rhodospirillum rubrum | 31969 | - |
| membrane | - |
Bacillus sp. PS3 | 16020 | - |
| mitochondrial membrane | - |
Rhodospirillum rubrum | 31966 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Rhodospirillum rubrum |  |
| Mg2+ | required | Bacillus sp. PS3 | |
| MgADP- | the reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | Rhodospirillum rubrum | |
| MgADP- | the reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | Bacillus sp. PS3 | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | Rhodospirillum rubrum | membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | Bacillus sp. PS3 | membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | ADP + phosphate + H+/out | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. PS3 | - |
- |
- |
| Rhodospirillum rubrum | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | - |
Rhodospirillum rubrum | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | - |
Bacillus sp. PS3 | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | Rhodospirillum rubrum | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | membrane de-energization makes ATP hydrolysis coupled with transmembrane proton transportation thermodynamically possible. This reaction slows down with time due to tight MgADP binding to one of the catalytic sites followed by slow reversible inactivation of the enzyme. Potency of tight MgADP binding and hence, that of enzyme inactivation, is substantially determined by asymmetric interaction between the gamma-subunit and the beta-subunits, overview. Enzymes lacking the gamma-subunit show no MgADP-induced inactivation | Bacillus sp. PS3 | ADP + phosphate + H+/out | - |
? | |
| additional information | transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview. Linking segments invovle residues Tyr345 with Arg356, Asp352 with Arg171, and Gln172 with Arg356, structures and interactions, overview | Rhodospirillum rubrum | ? | - |
? | |
| additional information | transduction of the conformation signal between catalytic and noncatalytic sites, linking segments involving e.g. residues are S344, G348 from one segment and S370, S372 from the other segment of the mitochondrial F1 alpha-subunit, interactions, overview | Bacillus sp. PS3 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview | Rhodospirillum rubrum |
| More | transduction of the conformation signal between catalytic and noncatalytic sites, overview | Bacillus sp. PS3 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| F1-ATPase | - |
Rhodospirillum rubrum |
| F1-ATPase | - |
Bacillus sp. PS3 |
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