Evidence map›Paper›PMID 21697092›Full record

ArticleThe Journal of biological chemistry2011

Structural basis of multifunctionality in a vitamin B12-processing enzyme.

Markos Koutmos, Carmen Gherasim, Janet L Smith, Ruma Banerjee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.3field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Review
  3. An unusual Co-S bond links BProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. The cobalamin processing enzyme of Trichoplax adhaerens.The Journal of biological chemistry · 2025
    Article
  5. Article
  6. Article
  7. Cobalt-Sulfur Coordination Chemistry Drives BJournal of the American Chemical Society · 2023
    Article
  8. meso-Bromination of cyano- and aquacobalamins facilitates their processing into Co(II)-species by glutathione.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023
    Article
  9. Article
  10. Review
  11. Bioprocess Strategies for Vitamin BBioengineering (Basel, Switzerland) · 2022
    Review
  12. Article
  13. The human BMethods in enzymology · 2022
    Article
  14. Article
  15. Redox-Linked Coordination Chemistry Directs Vitamin BAccounts of chemical research · 2021
    Article
  16. Mobile loop dynamics in adenosyltransferase control binding and reactivity of coenzyme BProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. An Interprotein Co-S Coordination Complex in the BJournal of the American Chemical Society · 2020
    Article
  20. The human BThe Journal of biological chemistry · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Markos KoutmosDepartment of Biological Chemistry and the Life Sciences Institute, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600, USA.
Carmen Gherasim
Janet L Smith
Ruma Banerjee
University of Michigan–Ann Arbor · US

Funding

REACTION MECHANISMS OF MAMMALIAN B12-DEPENDENT ENZYMESR01DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI RUMA V BANERJEE · 1998 to 2026
$9.7M
REGULATION OF FOLATE METABOLISMR01GM024908 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MATTHEWS, ROWENA G · 1985 to 2008
$2.9M
REGULATION TO FOLATE METABOLISMR37GM024908 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MATTHEWS, ROWENA G · 1991 to 2000
$327k
REACTION MECHANISMS OF COBALAMIN-DEPENDENT ENZYMESR29DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1993 to 1997
–
NCI NIH HHS Y1-CO-102NIDDK NIH HHS DK45776NIDDK NIH HHS R01 DK045776NIGMS NIH HHS GM024908NIGMS NIH HHS R01 GM024908NIGMS NIH HHS R37 GM024908NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

An early step in the intracellular processing of vitamin B(12) involves CblC, which exhibits dual reactivity, catalyzing the reductive decyanation of cyanocobalamin (vitamin B(12)), and the dealkylation of alkylcobalamins (e.g. methylcobalamin; MeCbl). Insights into how the CblC scaffold supports this chemical dichotomy have been unavailable despite it being the most common locus of patient mutations associated with inherited cobalamin disorders that manifest in both severe homocystinuria and methylmalonic aciduria. Herein, we report structures of human CblC, with and without bound MeCbl, which provide novel biochemical insights into its mechanism of action. Our results reveal that CblC is the most divergent member of the NADPH-dependent flavin reductase family and can use FMN or FAD as a prosthetic group to catalyze reductive decyanation. Furthermore, CblC is the first example of an enzyme with glutathione transferase activity that has a sequence and structure unrelated to the GST superfamily. CblC thus represents an example of evolutionary adaptation of a common structural platform to perform diverse chemistries. The CblC structure allows us to rationalize the biochemical basis of a number of pathological mutations associated with severe clinical phenotypes.

Indexed as

CatalysisCrystallography, X-RayFlavin-Adenine DinucleotideFlavin MononucleotideHumansHydrolasesProtein Structure, TertiaryStructure-Activity RelationshipVitamin B 12Flavin-Adenine DinucleotideFlavin MononucleotideHydrolasesVitamin B 12

Identifiers

PMID21697092
PMCPMC3191019
OpenAlexW1998188098

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.