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Merck

C0884

Sigma-Aldrich

Coenzyme B12

≥97.0%

Synonim(y):

5′-Deoxyadenosylcobalamine, Adenosyl cobalamine, Cobamamide, DMBC coenzyme

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About This Item

Wzór empiryczny (zapis Hilla):
C72H100CoN18O17P
Numer CAS:
Masa cząsteczkowa:
1579.58
Beilstein:
4122932
Numer WE:
Numer MDL:
Kod UNSPSC:
12352205
Identyfikator substancji w PubChem:
NACRES:
NA.79

Próba

≥97.0%

Postać

powder and chunks

metody

HPLC: suitable

kolor

red to very dark red
very dark red-brown

temp. przechowywania

−20°C

ciąg SMILES

CC(CNC(=O)CCC1(C)C(CC(N)=O)C2N([Co+]C[C@H]3O[C@@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)C1=C(C)C6=NC(=CC7=NC(=C(C)C8=NC2(C)C(C)(CC(N)=O)C8CCC(N)=O)C(C)(CC(N)=O)C7CCC(N)=O)C(C)(C)C6CCC(N)=O)OP([O-])(=O)O[C@H]9[C@@H](O)[C@H](O[C@@H]9CO)n%10cnc%11cc(C)c(C)cc%10%11

InChI

1S/C62H90N13O14P.C10H12N5O3.Co/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;1-4-6(16)7(17)10(18-4)15-3-14-5-8(11)12-2-13-9(5)15;/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);2-4,6-7,10,16-17H,1H2,(H2,11,12,13);/q;;+2/p-2/t31?,34?,35?,36?,37?,41-,52-,53-,56?,57+,59?,60?,61?,62?;4-,6-,7-,10+;/m11./s1

Klucz InChI

ZIHHMGTYZOSFRC-PMDPKNCCSA-L

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Opis ogólny

Vitamin B12 cobalamin refers to a group of chemically-related cobalt containing molecules. The physiologically active forms of vitamin B12 include methylcobalamin and adenosylcobalamin, whereas hydroxocobalamin (vitamin B12a, OHCbl) and cyanocobalamin (CNCbl) are storage and delivery forms.

Zastosowanie

Coenzyme B12 has been used as a supplement for culturing plasmid variants in in vivo assay of yvrC-lacZ fusions.

Działania biochem./fizjol.

Vitamin B12 cobalamin is involved in DNA synthesis and fatty acid synthesis. It also plays a vital role as a coenzyme in the conversion of mitochondrial methylmalonyl co-enzyme A to succinyl co-enzyme A.
This page may contain text that has been machine translated.

Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

Poszukaj Certyfikaty analizy (CoA), wpisując numer partii/serii produktów. Numery serii i partii można znaleźć na etykiecie produktu po słowach „seria” lub „partia”.

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Alla Peselis et al.
Nature structural & molecular biology, 19(11), 1182-1184 (2012-10-16)
Coenzyme B(12) has a key role in various enzymatic reactions and controls expression of bacterial genes through riboswitches. Here we report the crystal structure of the Symbiobacterium thermophilum B(12) riboswitch bound to its ligand adenosylcobalamin. The riboswitch forms a unique
J R Roth et al.
Annual review of microbiology, 50, 137-181 (1996-01-01)
This review examines deoxyadenosylcobalamin (Ado-B12) biosynthesis, transport, use, and uneven distribution among living forms. We describe how genetic analysis of enteric bacteria has contributed to these issues. Two pathways for corrin ring formation have been found-an aerobic pathway (in P.
Denis Bucher et al.
Journal of the American Chemical Society, 134(3), 1591-1599 (2012-01-11)
Vitamin B(12) and its biologically active counterparts possess the only examples of carbon-cobalt bonds in living systems. The role of such motifs as radical reservoirs has potential application in future catalytic and electronic nanodevices. To fully understand radical generation in
Peter Friedrich et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 18(50), 16114-16122 (2012-10-20)
Coenzyme B(12) can assist radical enzymes that accomplish the vicinal interchange of a hydrogen atom with a functional group. It has been proposed that the Co-C bond homolysis of coenzyme B(12) to cob(II)alamin and the 5'-deoxyadenosyl radical is aided by hydrogen bonding
Jiayun Pang et al.
Journal of the American Chemical Society, 134(4), 2367-2377 (2012-01-14)
We present here an energetic and atomistic description of how D-ornithine 4,5-aminomutase (OAM), an adenosylcobalamin (AdoCbl; coenzyme B(12))-dependent isomerase, employs a large-scale protein domain conformational change to orchestrate the homolytic rupture of the Co-C bond. Our results suggest that in

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