Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activity

11 Dec 2013

Abstract excerpt

CLYBL is a human mitochondrial enzyme of unknown function that is found in multiple eukaryotic taxa and conserved to bacteria. The protein is expressed in the mitochondria of all mammalian organs, with highest expression in brown fat and kidney. Approximately 5% of all humans harbor a premature stop polymorphism in CLYBL that has been associated with reduced levels of circulating vitamin B12. Using comparative...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Folate and B Vitamins Research
Share to Metabolism and Genetic Disorders
Share to Porphyrin Metabolism and Disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 24334609
DOI: 10.1093/hmg/ddt624

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CLYBL is a polymorphic human enzyme with malate synthase and β-methylmalate synthase activityPMID 24334609Read ↗

Genetics of MDH in humans.Semantic proximity Read ↗

Holocarboxylase synthetase deficiency: pathogenesis, clinical features, diagnosis, treatment, and research prospects.Semantic proximity Read ↗

Analyses of the genetic diversity and protein expression variation of the acyl: CoA medium-chain ligases, ACSM2A and ACSM2B.Semantic proximity Read ↗

The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency.Semantic proximity Read ↗

Spectrum and characterization of bi-allelic variants in MMAB causing cblB-type methylmalonic aciduria.Semantic proximity Read ↗

Functional and structural analysis of five mutations identified in methylmalonic aciduria cblB type.Semantic proximity Read ↗

Easily Misdiagnosed cblC Deficiency in Adolescents: the Clinical and Metabolic StudiesSemantic proximity Read ↗

The Human Glyoxalase Gene Family in Health and DiseaseSemantic proximity Read ↗

Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1: New insights into between-species divergence in glyoxylate metabolism.Semantic proximity Read ↗

Versatile enzymology and heterogeneous phenotypes in cobalamin complementation type C diseaseSemantic proximity Read ↗

Molecular insights into primary hyperoxaluria Type I pathogenesisSemantic proximity Read ↗

Functional Assessment of Lipoyltransferase-1 Deficiency in Cells, Mice, and HumansSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.