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DraconiticBiochemistryBiomolecules · Catabolism · Biosynthesis · MetabolismMap

Data

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Human metabolism

Reactome's human metabolism drawn as one network. Each molecule has one home node; widely shared molecules also appear as dashed copies in other territories, linked from their details. .

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Metabolite; its structure appears as you zoom in
Reaction, arrow toward the product
Cofactors and co-substrates are written beside the reaction when you zoom in
Dashed ring: a copy of a widely shared molecule or cofactor in another territory or pathway
Compartment transfer of the molecule it is linked to
Binding, release or complex event; its proteins are named in its details
Outline: reactions mostly in the mitochondrion

Arrows follow Reactome's curated reaction direction.

MMAB adenosylates cob(I)alamin

2 ATP + 2 cob(II)alamin + FADH2 → 2 PPP + 2 AdoCbl + 3 H+ + FAD

Reactome: R-HSA-3159253
Compartment: mitochondrial matrix
Rhea: None recorded

Inputs

2 ATPCHEBI:30616, C10H12N5O13P3, mitochondrial matrix
2 cob(II)alaminCHEBI:16304, C62H88CoN13O14P, mitochondrial matrix
FADH2CHEBI:58307, C27H33N9O15P2, mitochondrial matrix

Outputs

2 PPPCHEBI:15266, mitochondrial matrix
2 AdoCblCHEBI:18408, C72H100CoN18O17P, mitochondrial matrix
3 H+CHEBI:15378, H, mitochondrial matrix
FADCHEBI:57692, C27H30N9O15P2, mitochondrial matrix

Catalysed by

corrinoid adenosyltransferase activity of 3xMMAB [mitochondrial matrix]EC 2.5.1.17

Literature

Redox-Linked Coordination Chemistry Directs Vitamin B 12 Trafficking Acc Chem Res, 2021
Sacrificial Cobalt-Carbon Bond Homolysis in Coenzyme B 12 as a Cofactor Conservation Strategy J Am Chem Soc, 2018
Functional characterization and mutation analysis of human ATP:Cob(I)alamin adenosyltransferase Biochemistry, 2008
Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements Proc. Natl. Acad. Sci. U.S.A., 2002
Identification of the human and bovine ATP:Cob(I)alamin adenosyltransferase cDNAs based on complementation of a bacterial mutant J. Biol. Chem., 2003
Spectroscopic evidence for the formation of a four-coordinate Co2+ cobalamin species upon binding to the human ATP:cobalamin adenosyltransferase J Am Chem Soc, 2005