Ontology highlight
ABSTRACT:
SUBMITTER: Aspatwar A
PROVIDER: S-EPMC6609565 | biostudies-literature | 2019 Jul
REPOSITORIES: biostudies-literature
Aspatwar Ashok A Tolvanen Martti E E MEE Schneider Hans-Peter HP Becker Holger M HM Narkilahti Susanna S Parkkila Seppo S Deitmer Joachim W JW
FEBS open bio 20190611 7
Carbonic anhydrases (CA) catalyze the reversible hydration of CO<sub>2</sub> to protons and bicarbonate and thereby play a fundamental role in the epithelial acid/base transport mechanisms serving fluid secretion and absorption for whole-body acid/base regulation. The three carbonic anhydrase-related proteins (CARPs) VIII, X, and XI, however, are catalytically inactive. Previous work has shown that some CA isoforms noncatalytically enhance lactate transport through various monocarboxylate transp ...[more]