TY - JOUR
T1 - Structural basis for the reversibility of proton pyrophosphatase
AU - Regmi, Kamesh C.
AU - Pizzio, Gaston A.
AU - Gaxiola, Roberto
PY - 2016/10/2
Y1 - 2016/10/2
N2 - Proton Pyrophosphatase (H+-PPase) is an evolutionarily conserved enzyme regarded as a bona fide vacuolar marker. However, H+-PPase also localizes at the plasma membrane of the phloem, where, evidence suggests that it functions as a Pyrophosphate Synthase and participates in phloem loading and photosynthate partitioning. We believe that this pyrophosphate synthesising function of H+-PPase is fundamentally rooted to its molecular structure, and here we postulate, on the basis of published crystal structures of membrane-bound pyrophosphatases, a plausible mechanism of pyrophosphate synthesis.
AB - Proton Pyrophosphatase (H+-PPase) is an evolutionarily conserved enzyme regarded as a bona fide vacuolar marker. However, H+-PPase also localizes at the plasma membrane of the phloem, where, evidence suggests that it functions as a Pyrophosphate Synthase and participates in phloem loading and photosynthate partitioning. We believe that this pyrophosphate synthesising function of H+-PPase is fundamentally rooted to its molecular structure, and here we postulate, on the basis of published crystal structures of membrane-bound pyrophosphatases, a plausible mechanism of pyrophosphate synthesis.
KW - Crystal structure
KW - Proton pyrophosphatase
KW - Pyrophosphate synthase
KW - Sodium pyrophosphatase
KW - Sodium/Proton pyrophosphatase
UR - http://www.scopus.com/inward/record.url?scp=85010274889&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85010274889&partnerID=8YFLogxK
U2 - 10.1080/15592324.2016.1231294
DO - 10.1080/15592324.2016.1231294
M3 - Article
C2 - 27611445
AN - SCOPUS:85010274889
SN - 1559-2316
VL - 11
SP - e1231294
JO - Plant signaling & behavior
JF - Plant signaling & behavior
IS - 10
ER -