How to differentiate Coenzyme and Prosthetic group [closed]








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Coenzyme is a non protein molecules which bind loosely with enzymes, its function is help catalytic reaction proper functioning.
Prosthetic group covalently and tightly bind with protein.As my understanding, I knew that the Heme group in hemoglobin is a good example explaining prosthetic group.
Here is my confusion:
1.Does Coenzyme and Prosthetic group both exist in Enzyme simultaneously?
2.Is there any example about Enzyme with prosthetic group?
3.Does Enzyme without Prothetic group affect catalytic reaction proceeding?




One example is the enzyme methionine synthase. It has vitamin B12 as a prosthetic group and S-adenosyl methionine as a cofactor. Without vitamin B12 present, you would expect no catalysis (in fact, the protein might not even fold properly). For some reading with interactive 3D figures, see <https://proteopedia.org/wiki/index.php/Methionine_synthase>.


According to IUPAC, these are the definitions of prosthetic group and cofactor:



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> Prosthetic group: A tightly bound, specific nonpolypeptide unit in a protein determining and involved in its biological activity. See also cofactor.
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> 
> Cofactor: An organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group).
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Source: [IUPAC Recommendations 1997](https://web.archive.org/web/20121128190330/http://www.chem.qmul.ac.uk/iupac/bioinorg/CD.html#34)


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