Methionine gamma-lyase

Details

Name
Methionine gamma-lyase
Kind
protein
Synonyms
  • 4.4.1.11
  • L-methioninase
Gene Name
mdeA
UniProtKB Entry
P13254Swiss-Prot
Organism
Pseudomonas putida
NCBI Taxonomy ID
303
Amino acid sequence
>lcl|BSEQ0017023|Methionine gamma-lyase
MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAGHFYS
RISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDEVLLGNTLYGCTFAF
LHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYFESPANPNMHMADIAGVAKIARKHG
ATVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLK
DMTGAVLSPHDAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQY
TLARQQMSQPGGMIAFELKGGIGAGRRFMNALQLFSRAVSLGDAESLAQHPASMTHSSYT
PEERAHYGISEGLVRLSVGLEDIDDLLADVQQALKASA
Number of residues
398
Molecular Weight
42626.335
Theoretical pI
6.7
GO Classification
Functions
methionine gamma-lyase activity / pyridoxal phosphate binding
General Function
Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia (PubMed:6742420, PubMed:8586629). Is involved in L-methionine catabolism (PubMed:9190812). In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L-homocysteine and its S-substituted derivatives, O-substituted-L-homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S-methyl-L-cysteine, and O-acetyl-L-serine (PubMed:22785484, PubMed:6742420). Also catalyzes deamination and gamma-addition reactions of L-vinylglycine (PubMed:6742420). Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively (PubMed:22785484, PubMed:6742420).
Specific Function
homocysteine desulfhydrase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0006258|1197 bp
ATGCACGGCTCCAACAAGCTCCCAGGATTTGCCACCCGCGCCATTCACCATGGCTACGAC
CCCCAGGACCACGGCGGCGCACTGGTGCCACCGGTCTACCAGACCGCGACGTTCACCTTC
CCCACCGTGGAATACGGCGCTGCGTGCTTTGCCGGCGAGCAGGCCGGGCATTTCTACAGC
CGCATCTCCAACCCCACCCTCAACCTGCTGGAAGCACGCATGGCCTCGCTGGAAGGCGGC
GAGGCCGGGCTGGCGCTGGCCTCGGGCATGGGGGCGATCACGTCCACGCTATGGACACTG
CTGCGCCCCGGTGACGAGGTGCTGCTGGGCAACACCCTGTACGGCTGCACCTTTGCCTTC
CTGCACCACGGCATCGGCGAGTTCGGGGTCAAGCTGCGCCATGTGGACATGGCCGACCTG
CAGGCACTGGAGGCGGCCATGACGCCGGCCACCCGGGTGATCTATTTCGAGTCGCCGGCC
AACCCCAACATGCACATGGCCGATATCGCCGGCGTGGCGAAGATTGCACGCAAGCACGGC
GCGACCGTGGTGGTCGACAACACCTACTGCACGCCGTACCTGCAACGGCCACTGGAGCTG
GGCGCCGACCTGGTGGTGCATTCGGCCACCAAGTACCTGAGCGGCCATGGCGACATCACT
GCTGGCATTGTGGTGGGCAGCCAGGCACTGGTGGACCGTATACGTCTGCAGGGCCTCAAG
GACATGACCGGTGCGGTGCTCTCGCCCCATGACGCCGCACTGTTGATGCGCGGCATCAAG
ACCCTCAACCTGCGCATGGACCGCCACTGCGCCAACGCTCAGGTGCTGGCCGAGTTCCTC
GCCCGGCAGCCGCAGGTGGAGCTGATCCATTACCCGGGCCTGGCGAGCTTCCCGCAGTAC
ACCCTGGCCCGCCAGCAGATGAGCCAGCCGGGCGGCATGATCGCCTTCGAACTCAAGGGC
GGCATCGGTGCCGGGCGGCGGTTCATGAACGCCCTGCAACTGTTCAGCCGCGCGGTGAGC
CTGGGCGATGCCGAGTCGCTGGCGCAGCACCCGGCAAGCATGACTCATTCCAGCTATACC
CCAGAGGAGCGTGCGCATTACGGCATCTCCGAGGGGCTGGTGCGGTTGTCGGTGGGGCTG
GAAGACATCGACGACCTGCTGGCCGATGTGCAACAGGCACTCAAGGCGAGTGCCTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP13254
UniProtKB Entry NameMEGL_PSEPU
GenBank Gene IDD88554
PDB ID(s)1GC0, 1GC2, 1PG8, 1UKJ, 2O7C, 3VK2, 3VK3, 3VK4
General References
  1. Inoue H, Inagaki K, Sugimoto M, Esaki N, Soda K, Tanaka H: Structural analysis of the L-methionine gamma-lyase gene from Pseudomonas putida. J Biochem. 1995 May;117(5):1120-5. [Article]
  2. Inoue H, Inagaki K, Eriguchi SI, Tamura T, Esaki N, Soda K, Tanaka H: Molecular characterization of the mde operon involved in L-methionine catabolism of Pseudomonas putida. J Bacteriol. 1997 Jun;179(12):3956-62. [Article]
  3. Nakayama T, Esaki N, Tanaka H, Soda K: Specific labeling of the essential cysteine residue of L-methionine gamma-lyase with a cofactor analogue, N-(bromoacetyl)pyridoxamine phosphate. Biochemistry. 1988 Mar 8;27(5):1587-91. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
N(6)-(pyridoxal phosphate)-L-lysineexperimentalunknowntargetDetails