KEGG ENZYME: 4.1.1.57

ENZYME: 4.1.1.57

Entry

EC 4.1.1.57                 Enzyme

Name

methionine decarboxylase;
L-methionine decarboxylase;
L-methionine carboxy-lyase;
L-methionine carboxy-lyase (3-methylthiopropanamine-forming);
mdc (gene name)

Class

Lyases;
Carbon-carbon lyases;
Carboxy-lyases

Sysname

L-methionine carboxy-lyase [3-(methylsulfanyl)propanamine-forming]

Reaction(IUBMB)

L-methionine = 3-(methylsulfanyl)propanamine + CO2 [RN:R00656]

Reaction(KEGG)

R00656

Substrate

L-methionine [CPD:C00073]

Product

3-(methylsulfanyl)propanamine [CPD:C03354];
CO2 [CPD:C00011]

Comment

A pyridoxal 5'-phosphate enzyme, identified in bacteria of the Streptomyces genus, the fern Dryopteris filix-mas, and the marine dinoflagellate Crypthecodinium cohnii. The expressed enzyme also has activity with L-2-aminohexanoate (L-norleucine) [5].

History

EC 4.1.1.57 created 1972

Reference

Authors

Hagino H, Nakayama K.

Title

Amino acid metabolism in microorganisms. Part IV. L-Methionine decarboxylase produced by Streptomyces strain.

Journal

Agric Biol Chem 32:727-733 (1968)

Reference

Authors

Misono H, Kawabata Y, Toyosato M, Yamamoto T, Soda K.

Title

Purification and properties of L-methionine decarboxylase of Streptomyces sp.

Journal

Bull Inst Chem Res, Kyoto Univ 58:323-333 (1980)

Reference

3 [PMID:2271523]

Authors

Stevenson DE, Akhtar M, Gani D.

Title

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.

Journal

Biochemistry 29:7631-47 (1990)
DOI:10.1021/bi00485a013

Reference

Authors

Kitaguchi H, Uchida A, Ishida Y.

Title

Purification and characterization of L-methionine decarboxylase from Crypthecodinium cohnii.

Journal

Fish Sci 65:613-617 (1999)

Reference

5 [PMID:28003434]

Authors

Hayashi M, Okada A, Yamamoto K, Okugochi T, Kusaka C, Kudou D, Nemoto M, Inagaki J, Hirose Y, Okajima T, Tamura T, Soda K, Inagaki K.

Title

Gene cloning, recombinant expression, purification and characterization of l-methionine decarboxylase from Streptomyces sp. 590.

Journal

J Biochem 161:389-398 (2017)
DOI:10.1093/jb/mvw083

Reference

6 [PMID:33452696]

Authors

Okawa A, Shiba T, Hayashi M, Onoue Y, Murota M, Sato D, Inagaki J, Tamura T, Harada S, Inagaki K.

Title

Structural basis for substrate specificity of l-methionine decarboxylase.

Journal

Protein Sci 30:663-677 (2021)
DOI:10.1002/pro.4027

Other DBs

ExplorEnz - The Enzyme Database:

4.1.1.57

IUBMB Enzyme Nomenclature:

4.1.1.57

ExPASy - ENZYME nomenclature database:

4.1.1.57

BRENDA, the Enzyme Database:

4.1.1.57

CAS:	37290-50-9

LinkDB

DBGET integrated database retrieval system