Molybdopterin molybdotransferase

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Molybdopterin molybdotransferase
Molybdopterin molybdotransferase
Identifiers
EC no.	2.10.1.1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PubMed	articles
NCBI	proteins

Molybdopterin molybdotransferase (EC 2.10.1.1, MoeA, Cnx1) is an enzyme with systematic name adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming).^[1]^[2]^[3] This enzyme catalyses the following chemical reaction

adenylyl-molybdopterin + molybdate

\rightleftharpoons

molybdenum cofactor + AMP

Catalyses the insertion of molybdenum into the ene-dithiol group of molybdopterin.

References

^ Nichols JD, Rajagopalan KV (March 2005). "In vitro molybdenum ligation to molybdopterin using purified components". The Journal of Biological Chemistry. 280 (9): 7817–22. doi:10.1074/jbc.M413783200. PMID 15632135.
^ Nichols JD, Xiang S, Schindelin H, Rajagopalan KV (January 2007). "Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft". Biochemistry. 46 (1): 78–86. doi:10.1021/bi061551q. PMC 1868504. PMID 17198377.
^ Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G (July 2006). "The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly". The Journal of Biological Chemistry. 281 (27): 18343–50. doi:10.1074/jbc.M601415200. PMID 16636046.

External links

Molybdopterin+molybdotransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Zdroj:https://en.wikipedia.org?pojem=Molybdopterin_molybdotransferase
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[1] Nichols JD, Rajagopalan KV (March 2005). "In vitro molybdenum ligation to molybdopterin using purified components". The Journal of Biological Chemistry. 280 (9): 7817–22. doi:10.1074/jbc.M413783200. PMID 15632135.

[2] Nichols JD, Xiang S, Schindelin H, Rajagopalan KV (January 2007). "Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft". Biochemistry. 46 (1): 78–86. doi:10.1021/bi061551q. PMC 1868504. PMID 17198377.

[3] Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G (July 2006). "The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly". The Journal of Biological Chemistry. 281 (27): 18343–50. doi:10.1074/jbc.M601415200. PMID 16636046.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)