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PDBsum entry 7cii
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PDB id:
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Lyase
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Title:
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Crystal structure of l-methionine decarboxylase from streptomyces sp.590 in complexed with l- methionine methyl ester (external aldimine form).
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Structure:
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L-methionine decarboxylase. Chain: a, b. Engineered: yes
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Source:
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Streptomyces sp. 590 ki-2014. Organism_taxid: 1510823. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.51Å
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R-factor:
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0.175
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R-free:
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0.196
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Authors:
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A.Okawa,T.Shiba,M.Hayashi,Y.Onoue,M.Murota,D.Sato,J.Inagaki,T.Tamura, S.Harada,K.Inagaki
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Key ref:
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A.Okawa
et al.
(2021).
Structural basis for substrate specificity of l-methionine decarboxylase.
Protein Sci,
30,
663-677.
PubMed id:
DOI:
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Date:
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07-Jul-20
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Release date:
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27-Jan-21
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PROCHECK
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Headers
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References
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A0A0G4DBU7
(A0A0G4DBU7_9ACTN) -
L-methionine decarboxylase from Streptomyces sp. 590 KI-2014
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Seq:
Struc:
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557 a.a.
518 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Enzyme class:
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E.C.4.1.1.57
- methionine decarboxylase.
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Reaction:
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L-methionine + H+ = 3-(methylsulfanyl)propanamine + CO2
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L-methionine
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+
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H(+)
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=
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3-(methylsulfanyl)propanamine
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+
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CO2
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Protein Sci
30:663-677
(2021)
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PubMed id:
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Structural basis for substrate specificity of l-methionine decarboxylase.
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A.Okawa,
T.Shiba,
M.Hayashi,
Y.Onoue,
M.Murota,
D.Sato,
J.Inagaki,
T.Tamura,
S.Harada,
K.Inagaki.
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ABSTRACT
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l -Methionine decarboxylase (MetDC) from Streptomyces sp. 590 is a vitamin
B6 -dependent enzyme and catalyzes the non-oxidative decarboxylation
of l -methionine to produce 3-methylthiopropylamine and carbon dioxide. We
present here the crystal structures of the ligand-free form of MetDC and of
several enzymatic reaction intermediates. Group II amino acid decarboxylases
have many residues in common around the active site but the residues surrounding
the side chain of the substrate differ. Based on information obtained from the
crystal structure, and mutational and biochemical experiments, we propose a key
role for Gln64 in determining the substrate specificity of MetDC, and for Tyr421
as the acid catalyst that participates in protonation after the decarboxylation
reaction.
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Links
