Sequence of PEPM_MYTED
EC Number:5.4.2.9
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
phosphoenolpyruvate = 3-phosphonopyruvate
Other sequences found for EC No. 5.4.2.9
General information:
Sequence
0 MSTKVKKTTQ LKQMLNSKDL EFIMEAHNGL SARIVQEAGF KGIWGSGLSV SAQLGVRDSN
60 EASWTQVVEV LEFMSDASDV PILLDADTGY GNFNNARRLV RKLEDRGVAG ACLEDKLFPK
120 TNSLHDGRAQ PLADIEEFAL KIKACKDSQT DPDFCIVARV EAFIAGWGLD EALKRAEAYR
180 NAGADAILMH SKKADPSDIE AFMKAWNNQG PVVIVPTKYY KTPTDHFRDM GVSMVIWANH
240 NLRASVSAIQ QTTKQIYDDQ SLVNVEDKIV SVKEIFRLQR DDELVQAEDK YLPKN
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
203653
Jia Y.,Lu Z.,Huang K.,Herzberg O.,Dunaway-Mariano D.
Insight into the mechanism of phosphoenolpyruvate mutase catalysis derived from site-directed mutagenesis studies of active site residues.
Biochemistry
38
14165-14173
1999
203654
Huang K.,Li Z.,Jia Y.,Dunaway-Mariano D.,Herzberg O.
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate.
Structure
7
539-548
1999
203655
Liu S.,Lu Z.,Jia Y.,Dunaway-Mariano D.,Herzberg O.
Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.
Biochemistry
41
10270-10276
2002
