Difference between revisions of "Part:BBa K3144004"
 
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<partinfo>BBa_K3144004 short</partinfo>
 
<partinfo>BBa_K3144004 short</partinfo>
  
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Chain A, Pyrophosphate-energized vacuolar membrane proton pump from Vigna radiata (Mung bean). Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H+-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H+-ATPase on the same membrane. It belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases.  
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Chain A, Pyrophosphate-energized vacuolar membrane proton pump from Vigna radiata (Mung bean). Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H+-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H+-ATPase on the same membrane. V-PPase belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases.  
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===Usage and Biology===
 
===Usage and Biology===
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V-PPase consists of a single polypeptide and exists as a dimmer of subunits of 71–80 kDa.  
 
V-PPase consists of a single polypeptide and exists as a dimmer of subunits of 71–80 kDa.  
  
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===References===
 
===References===
 
1. Wada, Y. Mutagenic Analysis of Functional Residues in Putative Substrate- binding Site and Acidic Domains of Vacuolar H ؉ -Pyrophosphatase * clude essential common motifs shared among the P-type. 276, 7654–7660 (2001).
 
1. Wada, Y. Mutagenic Analysis of Functional Residues in Putative Substrate- binding Site and Acidic Domains of Vacuolar H ؉ -Pyrophosphatase * clude essential common motifs shared among the P-type. 276, 7654–7660 (2001).
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2. Silva, P. & Gerós, H. Regulation by salt of vacuolar H + -ATPase and H + -pyrophosphatase activities and Na + /H + exchange. Plant Signal. Behav. 4, 718–726 (2009).
  
  

Latest revision as of 11:21, 20 October 2019


AVP channel from Vigna radiata

Chain A, Pyrophosphate-energized vacuolar membrane proton pump from Vigna radiata (Mung bean). Proton-translocating inorganic pyrophosphatase that contributes to the transtonoplast (from cytosol to vacuole lumen) H+-electrochemical potential difference. It establishes a proton gradient of similar and often greater magnitude than the H+-ATPase on the same membrane. V-PPase belongs to the fourth class of electrogenic proton pump in addition to the P-, F-, and V-type ATPases.


Usage and Biology

V-PPase consists of a single polypeptide and exists as a dimmer of subunits of 71–80 kDa.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 2019

References

1. Wada, Y. Mutagenic Analysis of Functional Residues in Putative Substrate- binding Site and Acidic Domains of Vacuolar H ؉ -Pyrophosphatase * clude essential common motifs shared among the P-type. 276, 7654–7660 (2001).

2. Silva, P. & Gerós, H. Regulation by salt of vacuolar H + -ATPase and H + -pyrophosphatase activities and Na + /H + exchange. Plant Signal. Behav. 4, 718–726 (2009).