Hydroxocobalamin (CED0006062)

Record Information
Version1.0
Creation Date2009-03-22 21:40:18 UTC
Update Date2026-05-14 16:24:38 UTC
Accession NumberCHEM000604
Identification
Common NameHydroxocobalamin
ClassSmall Molecule
Description
Hydroxocobalamin is an endogenous solid with the chemical formula C62H89CoN13O15P. Hydroxocobalamin belongs to the corrinoids, a subclass of tetrapyrroles and derivatives within the organic compounds. With an average molecular weight of 1,346 g/mol, Hydroxocobalamin is a heavy molecule. It is found in healthcare, pharmaceuticals, and veterinary products, specifically within antianemic preparations and unclassified therapeutic products. Exposure routes for the compound include intramuscular, intravenous, and oral administration. Hydroxocobalamin is one of four major forms of vitamin B12, alongside cyanocobalamin, methylcobalamin, and deoxyadenosylcobalamin. It interacts with several protein targets, including Transcobalamin-1 (TCN1), Transcobalamin-2 (TCN2), Protein amnionless (AMN), and Methylmalonic aciduria type A protein, mitochondrial (MMAA). Additionally, cobalt inhibits heme synthesis by preventing the synthesis of 5-aminolaevulinate through the inhibition of 5-aminolevulinate synthase, non-specific, mitochondrial (ALAS1) and 5-aminolevulinate synthase, erythroid-specific, mitochondrial (ALAS2). Cobalt also inhibits carbonic anhydrases 1, 2, and 4 (CA1, CA2, CA4). Further interactions involve cobalt blocking high-voltage-activated calcium channels, including Voltage-dependent L-type calcium channel subunit beta-1 (CACNB1) and subunits alpha-1C, alpha-1D, and alpha-1S (CACNA1C, CACNA1D, CACNA1S), which may impair neurotransmission. Cobalt interacts with specific IgA antibodies (IGHA1, IGHA2) and specific IgE antibodies, resulting in immunosensitization. Furthermore, cobalt inhibits DNA repair by interacting with zinc finger DNA repair proteins such as Poly [ADP-ribose] polymerase 1 (PARP1). Radioactive cobalt also damages lipids, RNA, and DNA through ionizing events.
Contaminant Type
  • Amide
  • Amine
  • Anti-Anemic Agent
  • Cobalt Compound
  • Drug
  • Ether
  • Food Toxin
  • Hematinic
  • Human Neurotoxin
  • Metabolite
  • Natural Compound
  • Nutritional Supplement
  • Nutritional Support
  • Organic Compound
  • Pollutant
  • Vitamin B Complex
Chemical Structure
Synonyms
ValueSource
HydroxycobalaminChEBI
OH-CBLChEBI
Vitamin b-12bChEBI
HydroxominHMDB
Hydroxo-cobalaminHMDB
a-(5,6-Dimethylbenzimidazolyl)hydroxocobamideHMDB
alpha CobioneHMDB
alpha-(5,6-Dimethylbenzimidazolyl)hydroxocobamideHMDB
AxlonHMDB
Ciplamin HHMDB
CobalexHMDB
Cobalin HHMDB
Cobinamide hydroxide phosphate 3'-ester with 5,6-dimethyl-1-a-D-ribofuranosylbenzimidazole inner saltHMDB
Cobinamide hydroxide phosphate 3'-ester with 5,6-dimethyl-1-alpha-delta-ribofuranosylbenzimidazole inner saltHMDB
CodroxominHMDB
DocclanHMDB
DocelanHMDB
DocevitaHMDB
DroxominHMDB
Ducobee hyHMDB
DuradoceHMDB
Duralta-12HMDB
HydrocobalaminHMDB
HydrogrisevitHMDB
HydrovitHMDB
HydroxocobalamineHMDB
HydroxocobalaminHMDB
Chemical FormulaC62H89CoN13O15P
Average Molecular Mass1346.355 g/mol
Monoisotopic Mass1345.567 g/mol
CAS Registry Number13422-51-0
IUPAC Name(10S,12R,13S,17R,23R,24R,25R,30S,35S,36S,40S,41S,42R,46R)-30,35,40-tris(2-carbamoylethyl)-24,36,41-tris(carbamoylmethyl)-1,46-dihydroxy-12-(hydroxymethyl)-5,6,17,23,28,31,31,36,38,41,42-undecamethyl-15,20-dioxo-11,14,16-trioxa-2lambda5,9,19,26,43lambda5,44lambda5,45lambda5-heptaaza-15lambda5-phospha-1-cobaltadodecacyclo[27.14.1.1^{1,34}.1^{2,9}.1^{10,13}.0^{1,26}.0^{3,8}.0^{23,27}.0^{25,42}.0^{32,44}.0^{39,43}.0^{37,45}]heptatetraconta-2(47),3,5,7,27,29(44),32,34(45),37,39(43)-decaene-2,43,44,45-tetrakis(ylium)-1,1,1-triuid-15-olate
Traditional Name(10S,12R,13S,17R,23R,24R,25R,30S,35S,36S,40S,41S,42R,46R)-30,35,40-tris(2-carbamoylethyl)-24,36,41-tris(carbamoylmethyl)-1,46-dihydroxy-12-(hydroxymethyl)-5,6,17,23,28,31,31,36,38,41,42-undecamethyl-15,20-dioxo-11,14,16-trioxa-2lambda5,9,19,26,43lambda5,44lambda5,45lambda5-heptaaza-15lambda5-phospha-1-cobaltadodecacyclo[27.14.1.1^{1,34}.1^{2,9}.1^{10,13}.0^{1,26}.0^{3,8}.0^{23,27}.0^{25,42}.0^{32,44}.0^{39,43}.0^{37,45}]heptatetraconta-2(47),3,5,7,27,29(44),32,34(45),37,39(43)-decaene-2,43,44,45-tetrakis(ylium)-1,1,1-triuid-15-olate
SMILES[H]O[Co+]N1\C2=C(C)/C3=N/C(=C\C4=N\C(=C(C)/C5=N[C@@](C)([C@@]1([H])[C@H](CC(=O)N)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(=O)([O-])O[C@H]1[C@@H](O)[C@H](O[C@@H]1CO)N1C=NC2=CC(C)=C(C)C=C12)[C@@](C)(CC(N)=O)[C@@H]5CCC(=O)N)\[C@@](C)(CC(=O)N)[C@@H]4CCC(=O)N)/C(C)(C)[C@@H]3CCC(=O)N
InChI IdentifierInChI=1S/C62H90N13O14P.Co.H2O/c1-29-20-39-40(21-30(29)2)75(28-70-39)57-52(84)53(41(27-76)87-57)89-90(85,86)88-31(3)26-69-49(83)18-19-59(8)37(22-46(66)80)56-62(11)61(10,25-48(68)82)36(14-17-45(65)79)51(74-62)33(5)55-60(9,24-47(67)81)34(12-15-43(63)77)38(71-55)23-42-58(6,7)35(13-16-44(64)78)50(72-42)32(4)54(59)73-56;;/h20-21,23,28,31,34-37,41,52-53,56-57,76,84H,12-19,22,24-27H2,1-11H3,(H15,63,64,65,66,67,68,69,71,72,73,74,77,78,79,80,81,82,83,85,86);;1H2/q;+3;/p-3/t31-,34-,35-,36-,37+,41-,52-,53-,56-,57+,59-,60+,61+,62+;;/m1../s1
InChI KeyYOZNUFWCRFCGIH-WZHZPDAFSA-K
Chemical Taxonomy
Description Belongs to the class of organic compounds known as cobalamin derivatives. These are organic compounds containing a corrin ring, a cobalt atom, an a nucleotide moiety. Cobalamin Derivatives are actually derived from vitamin B12.
KingdomOrganic compounds
Super ClassOrganoheterocyclic compounds
ClassTetrapyrroles and derivatives
Sub ClassCorrinoids
Direct ParentCobalamin derivatives
Alternative Parents
Substituents
  • Cobalamin
  • Metallotetrapyrrole skeleton
  • 1-ribofuranosylbenzimidazole
  • Pentose phosphate
  • Glycosyl compound
  • N-glycosyl compound
  • Pentose monosaccharide
  • Monosaccharide phosphate
  • Benzimidazole
  • Phosphoethanolamine
  • Dialkyl phosphate
  • Fatty acyl
  • N-substituted imidazole
  • Organic phosphoric acid derivative
  • Benzenoid
  • Fatty amide
  • Alkyl phosphate
  • Phosphoric acid ester
  • Monosaccharide
  • Imidazole
  • Heteroaromatic compound
  • Pyrrolidine
  • Tetrahydrofuran
  • Azole
  • Pyrroline
  • Carboxamide group
  • Ketimine
  • Secondary carboxylic acid amide
  • Secondary alcohol
  • Primary carboxylic acid amide
  • Propargyl-type 1,3-dipolar organic compound
  • Carboxylic acid derivative
  • Oxacycle
  • Organic 1,3-dipolar compound
  • Azacycle
  • Organic metal salt
  • Organic transition metal salt
  • Carbonyl group
  • Organic cobalt salt
  • Imine
  • Organic salt
  • Organonitrogen compound
  • Hydrocarbon derivative
  • Organic oxide
  • Organopnictogen compound
  • Organooxygen compound
  • Alcohol
  • Organic zwitterion
  • Organic nitrogen compound
  • Organic oxygen compound
  • Primary alcohol
  • Aromatic heteropolycyclic compound
Molecular FrameworkAromatic heteropolycyclic compounds
External Descriptors
Biological Properties
StatusDetected and Not Quantified
OriginEndogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Membrane
Biofluid LocationsNot Available
Tissue LocationsNot Available
ApplicationsNot Available
Biological RolesNot Available
Chemical RolesNot Available
Organoleptic EffectsNot Available
Physical Properties
StateSolid
AppearanceRed crystals.
Experimental Properties
PropertyValue
Melting PointNot Available
Boiling PointNot Available
Solubility1.46e-02 g/L
Predicted Properties
PropertyValueSource
logP-14ChemAxon
pKa (Strongest Acidic)1.82ChemAxon
pKa (Strongest Basic)-0.55ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count14ChemAxon
Hydrogen Donor Count10ChemAxon
Polar Surface Area437.23 ŲChemAxon
Rotatable Bond Count16ChemAxon
Refractivity340.03 m³·mol⁻¹ChemAxon
Polarizability135.56 ųChemAxon
Number of Rings12ChemAxon
BioavailabilityNoChemAxon
Rule of FiveNoChemAxon
Ghose FilterNoChemAxon
Veber's RuleNoChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyDeposition DateView
LC-MS/MSLC-MS/MS Spectrumsplash10-000i-2120000009-a1a6c934c09c0655b549Not AvailableView Spectrum
LC-MS/MSLC-MS/MS Spectrumsplash10-0f79-4240000029-c4f23872a45ca99d454cNot AvailableView Spectrum
LC-MS/MSLC-MS/MS Spectrumsplash10-0f79-5240000139-aa3cc38ae6fc78c5c9d7Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-1404000009-d95c227e0c2a01a825adNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-2902000005-61bd391f47e0b9c2ba4bNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-3930000015-9f00c742a0c9e52997c4Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-000e-2509000000-5c630ca334aea70d2a2dNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-1900000000-be3cf15d7ba2b2a92d24Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0002-1900000000-545dabccb8cd6ce30e09Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-01ta-0019000000-46cfd5a0cb69ba348e42Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-002b-0059000000-376196659960214456efNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-02vi-1091000000-dbf9f840b7585cf446f5Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0006-0009000000-c6a17bec0ebfa0bd6c14Not AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0006-0098000000-e7699891d549a172871cNot AvailableView Spectrum
Predicted LC-MS/MSPredicted LC-MS/MS Spectrumsplash10-0006-0094000000-d1ca36a1a12f6b9d6c83Not AvailableView Spectrum
1D NMR13C NMR Spectrum (1D, D2O, predicted)Not AvailableNot AvailableView Spectrum
1D NMR1H NMR Spectrum (1D, D2O, predicted)Not AvailableNot AvailableView Spectrum
Toxicity Profile
Mechanism of ToxicityVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Carcinogenicity (IARC Classification)2B, possibly carcinogenic to humans. (6)
Minimum Risk LevelChronic Inhalation: 0.0001 mg/m3 (5) Intermediate Oral: 0.01 mg/kg/day (5)
SymptomsCobalt inhalation can cause asthma-like breathing problems. Skin contact is known to result in contact dermatitis, which is characterized by irritation and rashes. Ingesting large amounts of cobalt may cause nausea and vomiting. (11)
TreatmentTreatment of cobalt poisoning is symptomatic. (3)
Toxicity Values
Toxicity ValueUnitValue RangeOrganismDose DescriptorRoute of ExposurePredicted or ExperimentalReference
50.0mL/kg>50miceLD50i.v.experimentalL1865
Health Effects
Health EffectRelationshipDirectionReference
Exposure Sources
Source IDSourceSectorReference
276Antianemic preparationsHealthcare, pharmaceuticals & veterinary productsNot Available
409Unclassified therapeutic productsHealthcare, pharmaceuticals & veterinary productsNot Available
Pathways
1 pathway
Targets
StructureProteinUniProt IDOrganismRelationshipDetails
Ribonuclease pancreatic structureClick to view 3D structureRibonuclease pancreaticP07998HumansPredicted (SEA)54.0274
Non-secretory ribonuclease structureClick to view 3D structureNon-secretory ribonucleaseP10153HumansPredicted (SEA)54.0274
Click to view 3D structureGlutamine--tRNA ligaseP00962Escherichia coli (strain K12)Predicted (SEA)60.9559
Click to view 3D structureHistone acetyltransferase GCN5Q245K9Tetrahymena thermophila (strain SB210)Predicted (SEA)120.433
Click to view 3D structureAminoglycoside acetyltransferaseQ70E71Enterococcus duransPredicted (SEA)38.0683
N-alpha-acetyltransferase 40 structureClick to view 3D structureN-alpha-acetyltransferase 40Q86UY6HumansPredicted (SEA)91.6285
1,4-dihydroxy-2-naphthoyl-CoA synthase structureClick to view 3D structure1,4-dihydroxy-2-naphthoyl-CoA synthaseP9WNP5Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)Predicted (SEA)56.2071
Click to view 3D structureS-adenosylmethionine synthase isoform type-1P13444Rattus norvegicusPredicted (SEA)57.1413
Click to view 3D structureAspartate--tRNA ligaseP21889Escherichia coli (strain K12)Predicted (SEA)72.3219
Histone-arginine methyltransferase CARM1 structureClick to view 3D structureHistone-arginine methyltransferase CARM1Q86X55HumansPredicted (SEA)1865.5
Click to view 3D structureAdenosine receptor A2aP30543Rattus norvegicusPredicted (SEA)4118.77
Click to view 3D structureProtein arginine N-methyltransferase 7Q9NVM4HumansPredicted (SEA)484.456
Adenosine receptor A2a structureClick to view 3D structureAdenosine receptor A2aP29274HumansPredicted (SEA)6218.44
Protein arginine N-methyltransferase 5 structureClick to view 3D structureProtein arginine N-methyltransferase 5O14744HumansPredicted (SEA)1231.34
Protein arginine N-methyltransferase 1 structureClick to view 3D structureProtein arginine N-methyltransferase 1Q99873HumansPredicted (SEA)1316.35
Protein arginine N-methyltransferase 8 structureClick to view 3D structureProtein arginine N-methyltransferase 8Q9NR22HumansPredicted (SEA)1061.71
Click to view 3D structure4-diphosphocytidyl-2-C-methyl-D-erythritol kinaseP62615Escherichia coli (strain K12)Predicted (SEA)207.312
Protein arginine N-methyltransferase 9 structureClick to view 3D structureProtein arginine N-methyltransferase 9Q6P2P2HumansPredicted (SEA)225.062
Click to view 3D structure2-dehydropantoate 2-reductaseP0A9J4Escherichia coli K-12Predicted (SEA)61.6566
Click to view 3D structureMet repressorC3SIU2Escherichia coliPredicted (SEA)92.952
Adenosine receptor A3 structureClick to view 3D structureAdenosine receptor A3P0DMS8HumansPredicted (SEA)6695.42
P2Y purinoceptor 1 structureClick to view 3D structureP2Y purinoceptor 1P47900HumansPredicted (SEA)1691.97
Adenosine receptor A1 structureClick to view 3D structureAdenosine receptor A1P30542HumansPredicted (SEA)6479.94
Click to view 3D structureSerine--tRNA ligaseP0A8L1Escherichia coli (strain K12)Predicted (SEA)80.9632
Click to view 3D structureBirA bifunctional proteinP96884Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)Predicted (SEA)75.5137
Methionine synthase structureClick to view 3D structureMethionine synthaseQ99707HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Methylmalonyl-CoA mutase, mitochondrial structureClick to view 3D structureMethylmalonyl-CoA mutase, mitochondrialP22033HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Transcobalamin-2 structureClick to view 3D structureTranscobalamin-2P20062HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Cyanocobalamin reductase / alkylcobalamin dealkylase structureClick to view 3D structureCyanocobalamin reductase / alkylcobalamin dealkylaseQ9Y4U1HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Carbonic anhydrase 1 structureClick to view 3D structureCarbonic anhydrase 1P00915HumansKnownCobalt inhibits carbonic anhydrases.(A38, A98)
Carbonic anhydrase 2 structureClick to view 3D structureCarbonic anhydrase 2P00918HumansKnownCobalt inhibits carbonic anhydrases.(A38, A98)
Carbonic anhydrase 4 structureClick to view 3D structureCarbonic anhydrase 4P22748HumansKnownCobalt inhibits carbonic anhydrases.(A38, A98)
Corrinoid adenosyltransferase MMAB structureClick to view 3D structureCorrinoid adenosyltransferase MMABQ96EY8HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Cubilin structureClick to view 3D structureCubilinO60494HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Methionine synthase reductase structureClick to view 3D structureMethionine synthase reductaseQ9UBK8HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Methylmalonic aciduria type A protein, mitochondrial structureClick to view 3D structureMethylmalonic aciduria type A protein, mitochondrialQ8IVH4HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Protein amnionless structureClick to view 3D structureProtein amnionlessQ9BXJ7HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
Transcobalamin-1 structureClick to view 3D structureTranscobalamin-1P20061HumansKnownVitamin B12 exists in four major forms referred to collectively as cobalamins; deoxyadenosylcobalamin, methylcobalamin, hydroxocobalamin, and cyanocobalamin. Two of these, methylcobalamin and 5-deoxyadenosyl cobalamin, are primarily used by the body. Methionine synthase needs methylcobalamin as a cofactor. This enzyme is involved in the conversion of the amino acid homocysteine into methionine. Methionine in turn is required for DNA methylation. 5-Deoxyadenosyl cobalamin is a cofactor needed by the enzyme that converts L-methylmalonyl-CoA to succinyl-CoA. This conversion is an important step in the extraction of energy from proteins and fats. Furthermore, succinyl CoA is necessary for the production of hemoglobin, the substances that carries oxygen in red blood cells.
5-aminolevulinate synthase, erythroid-specific, mitochondrial structureClick to view 3D structure5-aminolevulinate synthase, erythroid-specific, mitochondrialP22557HumansKnownCobalt inhibits heme synthesis by preventing synthesis of 5-aminolaevulinate via inhibition of 5-aminolaevulinate synthase. (L22)
Click to view 3D structure5-aminolevulinate synthase, non-specific, mitochondrialP13196HumansKnownCobalt inhibits heme synthesis by preventing synthesis of 5-aminolaevulinate via inhibition of 5-aminolaevulinate synthase. (L22)
Immunoglobulin heavy constant alpha 1 structureClick to view 3D structureImmunoglobulin heavy constant alpha 1P01876HumansKnownCobalt interacts with specific IgA antibodies, resulting in immunosensitization. (A102)
Immunoglobulin heavy constant alpha 2 structureClick to view 3D structureImmunoglobulin heavy constant alpha 2P01877HumansKnownCobalt interacts with specific IgA antibodies, resulting in immunosensitization. (A102)
Poly [ADP-ribose] polymerase 1 structureClick to view 3D structurePoly [ADP-ribose] polymerase 1P09874HumansKnownCobalt inhibits DNA repair by interacting with zinc finger DNA repair proteins. (A103)
Voltage-dependent L-type calcium channel subunit alpha-1C structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit alpha-1CQ13936HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit alpha-1D structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit alpha-1DQ01668HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Click to view 3D structureVoltage-dependent L-type calcium channel subunit alpha-1FO60840HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit alpha-1S structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit alpha-1SQ13698HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit beta-1 structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit beta-1Q02641HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit beta-2 structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit beta-2Q08289HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit beta-3 structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit beta-3P54284HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent L-type calcium channel subunit beta-4 structureClick to view 3D structureVoltage-dependent L-type calcium channel subunit beta-4O00305HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent N-type calcium channel subunit alpha-1B structureClick to view 3D structureVoltage-dependent N-type calcium channel subunit alpha-1BQ00975HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent P/Q-type calcium channel subunit alpha-1A structureClick to view 3D structureVoltage-dependent P/Q-type calcium channel subunit alpha-1AO00555HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Click to view 3D structureVoltage-dependent calcium channel gamma-1 subunitQ06432HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Voltage-dependent calcium channel subunit alpha-2/delta-1 structureClick to view 3D structureVoltage-dependent calcium channel subunit alpha-2/delta-1P54289HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Click to view 3D structureVoltage-dependent calcium channel subunit alpha-2/delta-2Q9NY47HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Click to view 3D structureVoltage-dependent calcium channel subunit alpha-2/delta-3Q8IZS8HumansKnownCobalt blocks high-voltage-activated calcium channels, possibly impairing neurotransmission. (A100)
Concentrations
Not Available
External Links
DrugBank IDDB00200
HMDB IDHMDB0002308
FooDB IDFDB003166
Phenol Explorer IDNot Available
KNApSAcK IDNot Available
BiGG IDNot Available
BioCyc IDNot Available
METLIN ID6607
PDB IDNot Available
Wikipedia LinkHydroxocobalamin
Chemspider ID28534326
ChEBI ID27786
PubChem Compound ID15589840
Kegg Compound IDC08230
YMDB IDNot Available
ECMDB IDNot Available
References
Synthesis Reference

Takayuki Hirayama, Takashi Kiyota, “Process for production of hydroxocobalamin.” U.S. Patent US5338418, issued June, 1982.

MSDSLink
General References
1. Van den Berg MP, Merkus P, Romeijn SG, Verhoef JC, Merkus FW: Hydroxocobalamin uptake into the cerebrospinal fluid after nasal and intravenous delivery in rats and humans. J Drug Target. 2003 Jul;11(6):325-31.
2. Fahmy NR: Consumption of vitamin B12 during sodium nitroprusside administration in humans. Anesthesiology. 1981 Apr;54(4):305-9.
3. Weinberg JB, Sauls DL, Misukonis MA, Shugars DC: Inhibition of productive human immunodeficiency virus-1 infection by cobalamins. Blood. 1995 Aug 15;86(4):1281-7.
4. Begley JA, Colligan PD, Chu RC: Transcobalamin II mediated delivery of albumin-bound hydroxocobalamin to human liver cells. Proc Soc Exp Biol Med. 1993 Nov;204(2):206-10.
5. van Kapel J, Spijkers LJ, Lindemans J, Abels J: Improved distribution analysis of cobalamins and cobalamin analogues in human plasma in which the use of thiol-blocking agents is a prerequisite. Clin Chim Acta. 1983 Jul 15;131(3):211-24.
6. Andersson HC, Shapira E: Biochemical and clinical response to hydroxocobalamin versus cyanocobalamin treatment in patients with methylmalonic acidemia and homocystinuria (cblC). J Pediatr. 1998 Jan;132(1):121-4.
7. el Kholty S, Gueant JL, Bressler L, Djalali M, Boissel P, Gerard P, Nicolas JP: Portal and biliary phases of enterohepatic circulation of corrinoids in humans. Gastroenterology. 1991 Nov;101(5):1399-408.
8. Seetharam B, Yammani RR: Cobalamin transport proteins and their cell-surface receptors. Expert Rev Mol Med. 2003 Jun 13;5(18):1-18.