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4.1.1.57 |
Description |
Methionine decarboxylase |
Alternative names |
L-methionine decarboxylase. |
Catalyzed reaction |
L-methionine = 3-methylthiopropanamine + CO(2). |
Cofactor |
Pyridoxal-phosphate. |
Organisms |
-Eubacteria -Plants |
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Links |
Enzyme (activities) 4.1.1.57
BRENDA (activities) 4.1.1.57
KEGG (pathways) 4.1.1.57
PLPMDB (PLP mutants) 4.1.1.57
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References |
Hayashi M, Okada A, Yamamoto K1, Okugochi T, Kusaka C, Kudou D, Nemoto M, Inagaki J, Hirose Y, Okajima T, Tamura T, Soda K, Inagaki K (2017) Gene cloning, recombinant expression, purification and characterization of l-methionine decarboxylase from Streptomyces sp. 590. J Biochem (Tokyo) 161 389-98. Kitaguchi, H.; Uchida, A.; Ishida, Y. (1999) Purification and characterization of L-methionine decarboxylase from Crypthecodinium cohnii Fish Sci 65 613-617. Stevenson, D. E.; Akhtar, M.; Gani, D. (1990) L-methionine decarboxylase from Dryopteris filix-mas: purification, characterization, substrate specificity, abortive transamination of the coenzyme, and stereochemical courses of substrate decarboxylation and coenzyme transamination Biochemistry 29 7631-47. Hagino, H.; Nakayama, K. (1968) Amino acid metabolism in microorganisms. Part IV. L-Methionine decarboxylase produced by a Streptomyces strain Agric Biol Chem 32 727-733. Articles on 4.1.1.57 |
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last changed |
2019/06/21 13:10 |
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