Sequence of Q84AR1_CITFR
EC Number:4.4.1.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
an S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate
General information:
Sequence
0 MSDCRTYGFN TQIVHAGQQP DPSTGALSTP IFQTSTFVFD SAEQGAARFA LEESGYIYTR
60 LGNPTTDALE KKLAVLERGE AGLATASGIS AITTTLLTLC QQGDHIVSAS AIYGCTHAFL
120 SHSMPKFGIN VRLVDAGKPE EIRAAMRPET KVVYIETPAN PTLSLVDIET VAGIAHQQGA
180 LLVVDNTFMS PYCQQPLQLG ADIVVHSVTK YINGHGDVIG GIIVGKQEFI DQARFVGLKD
240 ITGGCMSPFN AWLTLRGVKT LGIRMERHCE NALKIARFLE GHPSITRVYY PGLSSHPQYE
300 LGQRQMSLPG GIISFEIAGG LEAGRRMINS VELCLLAVSL GDTETLIQHP ASMTHSPVAP
360 EERLKAGITD GLIRLSVGLE DPEDIINDLE HAIRKATF
Download this sequence
in fasta formatDownload all sequences for 4.4.1.4
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
233813182
Mamaeva D.V.,Morozova E.A.,Nikulin A.D.,Revtovich S.V.,Nikonov S.V.,Garber M.B.,Demidkina T.V.
Structure of Citrobacter freundii L-methionine gamma-lyase.
Acta Crystallogr. F
61
546-549
2005
233813183
Manukhov I.V.,Mamaeva D.V.,Rastorguev S.M.,Faleev N.G.,Morozova E.A.,Demidkina T.V.,Zavilgelsky G.B.
A gene encoding L-methionine gamma-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine gamma-lyase.
J. Bacteriol.
187
3889-3893
2005
233813184
Nikulin A.,Revtovich S.,Morozova E.,Nevskaya N.,Nikonov S.,Garber M.,Demidkina T.
High-resolution structure of methionine gamma-lyase from Citrobacter freundii.
Acta Crystallogr. D
64
211-218
2008
233813185
Revtovich S.V.,Morozova E.A.,Khurs E.N.,Zakomirdina L.N.,Nikulin A.D.,Demidkina T.V.,Khomutov R.M.
Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates.
Biochemistry (Mosc.)
76
564-570
2011
233813186
Ronda L.,Bazhulina N.P.,Morozova E.A.,Revtovich S.V.,Chekhov V.O.,Nikulin A.D.,Demidkina T.V.,Mozzarelli A.
Exploring methionine gamma-lyase structure-function relationship via microspectrophotometry and X-ray crystallography.
Biochim. Biophys. Acta
1814
834-842
2011
233813187
Morozova E.A.,Revtovich S.V.,Anufrieva N.V.,Kulikova V.V.,Nikulin A.D.,Demidkina T.V.
Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.
Acta Crystallogr. D
70
3034-3042
2014
233813188
Revtovich S.V.,Faleev N.G.,Morozova E.A.,Anufrieva N.V.,Nikulin A.D.,Demidkina T.V.
Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors.
Biochimie
101
161-167
2014
233813189
Kuznetsov N.A.,Faleev N.G.,Kuznetsova A.A.,Morozova E.A.,Revtovich S.V.,Anufrieva N.V.,Nikulin A.D.,Fedorova O.S.,Demidkina T.V.
Pre-steady-state kinetic and structural analysis of interaction of methionine gamma-lyase from Citrobacter freundii with inhibitors.
J. Biol. Chem.
290
671-681
2015
