Coenzyme B12 (hydrate)
(Synonyms: Adenosylcobalamin, AdoCbl, Cobamamide, Dibenzcozamide, LM-176) 目录号 : GC47115
A neuropeptide with diverse biological activities
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
Coenzyme B12 (adenosylcobalamin; AdoCbl) is a biologically active form of vitamin B12 . It belongs to the corrinoid group of compounds, which contain a corrin macrocycle, and is produced only by certain bacteria and archaea.1 It is a cofactor for various enzymes including mutases, eliminases, aminomutases, and a reductase.2 These enzymes catalyze reactions that generate free radicals through release of the adenosyl group, allowing usually unreactive molecules to become reactive. Only one of these enzymes, methylmalonyl CoA mutase, is found in mammals, therefore, the other enzymes must be taken in through the diet. Genetic mutations in enzymes that synthesize AdoCbl lead to AdoCbl deficiency and methylmalonic aciduria.3 Formulations containing AdoCbl are used to treat patients with this disorder.
1.Moore, S.J., Lawrence, A.D., Biedendieck, R., et al.Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B12)Proc. Natl. Acad. Sci. USA110(37)14906-14911(2015) 2.Marsh, E.N.G., and MelÉndez, G.D.R.Adenosylcobalamin enzymes: Theory and experiment begin to convergeBiochim Biophys. Acta.1824(11)1154-1164(2012) 3.Watkins, D.N., Rosenblatt, D.S., and Flower, B.Adenosylcobalamin deficiencyInborn metabolic diseases: Diagnosis and treatment(2016)
| Cas No. | N/A | SDF | |
| 别名 | Adenosylcobalamin, AdoCbl, Cobamamide, Dibenzcozamide, LM-176 | ||
| Canonical SMILES | O[C@@H]1[C@H](O[C@@H](N2C3=NC=NC(N)=C3N=C2)[C@@H]1O)[CH2-][Co+3]456([N]7=CN([C@]8([H])[C@H](O)[C@H](O9)[C@@H](CO)O8)C%10=CC(C)=C(C)C=C7%10)[N]%11=C%12[C@@H](CCC(N)=O)[C@@](CC(N)=O)(C)[C@]%11(C)[C@]([C@H](CC(N)=O)[C@]%13(CCC(NC[C@@H](C)O[P]9([O-])=O)=O)C)([H])[N-]4C%13=C(C)C([C@@H](CCC(N)=O)C%14(C)C)=[N]5C%14=CC%15=[N]6C([C@](CC(N)=O)(C)[C@@H]%15CCC(N)=O)=C%12C.O | ||
| 分子式 | C72H100CoN18O17P.XH2O | 分子量 | 1579.6 |
| 溶解度 | DMSO: soluble,Ethanol: soluble,Water: soluble | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.6331 mL | 3.1654 mL | 6.3307 mL |
| 5 mM | 0.1266 mL | 0.6331 mL | 1.2661 mL |
| 10 mM | 0.0633 mL | 0.3165 mL | 0.6331 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Substrate-induced radical formation in 4-hydroxybutyryl coenzyme A dehydratase from Clostridium aminobutyricum
Appl Environ Microbiol 2015 Feb;81(3):1071-84.PMID:25452282DOI:10.1128/AEM.03099-14.
4-Hydroxybutyryl-coenzyme A (CoA) dehydratase (4HBD) from Clostridium aminobutyricum catalyzes the reversible dehydration of 4-hydroxybutyryl-CoA to crotonyl-CoA and the irreversible isomerization of vinylacetyl-CoA to crotonyl-CoA. 4HBD is an oxygen-sensitive homotetrameric enzyme with one [4Fe-4S](2+) cluster and one flavin adenine dinucleotide (FAD) in each subunit. Upon the addition of crotonyl-CoA or the analogues butyryl-CoA, acetyl-CoA, and CoA, UV-visible light and electron paramagnetic resonance (EPR) spectroscopy revealed an internal one-electron transfer to FAD and the [4Fe-4S](2+) cluster prior to hydration. We describe an active recombinant 4HBD and variants produced in Escherichia coli. The variants of the cluster ligands (H292C [histidine at position 292 is replaced by cysteine], H292E, C99A, C103A, and C299A) had no measurable dehydratase activity and were composed of monomers, dimers, and tetramers. Variants of other potential catalytic residues were composed only of tetramers and exhibited either no measurable (E257Q, E455Q, and Y296W) hydratase activity or <1% (Y296F and T190V) dehydratase activity. The E455Q variant but not the Y296F or E257Q variant displayed the same spectral changes as the wild-type enzyme after the addition of crotonyl-CoA but at a much lower rate. The results suggest that upon the addition of a substrate, Y296 is deprotonated by E455 and reduces FAD to FADH·, aided by protonation from E257 via T190. In contrast to FADH·, the tyrosyl radical could not be detected by EPR spectroscopy. FADH· appears to initiate the radical dehydration via an allylic ketyl radical that was proposed 19 years ago. The mode of radical generation in 4HBD is without precedent in anaerobic radical chemistry. It differs largely from that in enzymes, which use Coenzyme B12, S-adenosylmethionine, ATP-driven electron transfer, or flavin-based electron bifurcation for this purpose.
The reaction of the substrate analog 2-ketoglutarate with adenosylcobalamin-dependent glutamate mutase
J Biol Chem 1999 Apr 23;274(17):11619-22.PMID:10206971DOI:10.1074/jbc.274.17.11619.
Glutamate mutase is one of several adenosylcobalamin-dependent enzymes that catalyze unusual rearrangements that proceed through a mechanism involving free radical intermediates. The enzyme exhibits remarkable specificity, and so far no molecules other than L-glutamate and L-threo-3-methylaspartate have been found to be substrates. Here we describe the reaction of glutamate mutase with the substrate analog, 2-ketoglutarate. Binding of 2-ketoglutarate (or its hydrate) to the holoenzyme elicits a change in the UV-visible spectrum consistent with the formation of cob(II)alamin on the enzyme. 2-ketoglutarate undergoes rapid exchange of tritium between the 5'-position of the coenzyme and C-4 of 2-ketoglutarate, consistent with the formation of a 2-ketoglutaryl radical analogous to that formed with glutamate. Under aerobic conditions this leads to the slow inactivation of the enzyme, presumably through reaction of free radical species with oxygen. Despite the formation of a substrate-like radical, no rearrangement of 2-ketoglutarate to 3-methyloxalacetate could be detected. The results indicate that formation of the C-4 radical of 2-ketoglutarate is a facile process but that it does not undergo further reactions, suggesting that this may be a useful substrate analog with which to investigate the mechanism of coenzyme homolysis.