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Article

Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases.

The Journal of biological chemistry - 4 Dec 2015

Yamada Kazuhiro, Gherasim Carmen, Banerjee Ruma, Koutmos Markos

Abstract excerpt

In mammals, B12 (or cobalamin) is an essential cofactor required by methionine synthase and methylmalonyl-CoA mutase. A complex intracellular pathway supports the assimilation of cobalamin into its active cofactor forms and delivery to its target enzymes. MMADHC (the methylmalonic aciduria and homocystinuria type D protein), commonly referred to as CblD, is a key chaperone involved in intracellular cobalamin...

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Source

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Identifiers

PMID: 26364851
DOI: 10.1074/jbc.M115.682435
PMCID: PMC4705922

Genes

MMADHC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases.PMID 26364851Read ↗

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Cobalt-sulfur coordination chemistry drives B <sub>12</sub> loading onto methionine synthaseSemantic proximity Read ↗

Structures of the Human GTPase MMAA and Vitamin B12-dependent Methylmalonyl-CoA Mutase and Insight into Their Complex FormationSemantic proximity Read ↗

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