NCU06005 is a glycerol-kinase-family enzyme predicted to phosphorylate glycerol with ATP, producing sn-glycerol-3-phosphate. This reaction initiates glycerol assimilation and supplies an intermediate for carbon and glycerolipid metabolism. Classical Neurospora crassa enzymology identifies a cytosolic glycerokinase in the inducible glycerol-dissimilation pathway; the precise correspondence of that historical glp-4 activity to the modern NCU06005 locus and any additional mitochondrial pool remain unresolved.
Summary: The glycerol-kinase-specific IPR005999 and PANTHER glycerol-kinase subfamily distinguish this enzyme from generic FGGY carbohydrate kinases. Classical N. crassa experiments establish glycerokinase-dependent glycerol utilization, grounding transfer of ATP-dependent glycerol phosphorylation; a modern target-specific purified assay was not recovered.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: The glycerol-kinase-specific IPR005999 and PANTHER glycerol-kinase subfamily distinguish this enzyme from generic FGGY carbohydrate kinases. Classical N. crassa experiments establish glycerokinase-dependent glycerol utilization, grounding transfer of ATP-dependent glycerol phosphorylation; a modern target-specific purified assay was not recovered.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: The mitochondrial IBA is an ancestral localization assertion at PTN000023394, but classical N. crassa enzymology identifies cytosolic glycerokinase and mitochondrial glycerol-3-phosphate dehydrogenase as separate activities. The historical glp-4 to NCU06005 mapping and any dual localization are not fully resolved, so the IBA is neither confirmed nor removed.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: Glycerol phosphorylation is the entry reaction of the experimentally characterized fungal glycerol-dissimilation pathway. Glycerol catabolism describes that established role more precisely than broad carbohydrate or glycerol metabolism.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: Glycerol phosphorylation is the entry reaction of the experimentally characterized fungal glycerol-dissimilation pathway. Glycerol catabolism describes that established role more precisely than broad carbohydrate or glycerol metabolism.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: The kinase produces glycerol-3-phosphate directly, supporting its biosynthetic process rather than unspecified metabolism of that intermediate.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: Glycerol kinase supplies glycerol-3-phosphate, a glycerolipid precursor, so the curated triglyceride-metabolism inference is a plausible downstream role. It does not make this enzyme a triglyceride synthase, and target lipid flux was not measured in the retrieved glycerol-utilization studies.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
GO:0016773 phosphotransferase activity, alcohol group as acceptor
IEA GO_REF:0000002
MODIFY
Summary: The diagnostic glycerol-kinase family resolves the phosphoryl acceptor as glycerol and supports the specific kinase activity.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Summary: ATP-dependent glycerol phosphorylation both initiates glycerol catabolism and directly produces glycerol-3-phosphate. The specific family assignment and classical fungal glycerol-utilization enzymology support this process.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
GO:0046167 glycerol-3-phosphate biosynthetic process
IBA GO_REF:0000033
ACCEPT
Summary: ATP-dependent glycerol phosphorylation both initiates glycerol catabolism and directly produces glycerol-3-phosphate. The specific family assignment and classical fungal glycerol-utilization enzymology support this process.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
Core Functions
Phosphorylates glycerol with ATP to form sn-glycerol-3-phosphate.
Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
Review rationale: The glycerol-kinase-specific family assignment and classical N. crassa glycerol-dissimilation enzymology ground transfer of glycerol phosphorylation. This directly produces glycerol-3-phosphate, supporting the existing biosynthetic-process annotation. The predicted metabolic process is biologically correct but less precise than biosynthesis.
PMID:6284716: "Evidence from the enzymatic characterization of these mutants indicated that glp-2 and glp-4 were the structural genes encoding the mitochondrial glycerol-3-phosphate dehydrogenase and cytosolic glycerokinase, respectively."