Sequence of PCHB_PSEAE
EC Number:4.1.99
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Q51507
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
101
11432
Reaction
Other sequences found for EC No. 4.1.99
EC Number:4.2.99.21
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
isochorismate lyase
Q51507
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
101
11432
Reaction
isochorismate = salicylate + pyruvate
Other sequences found for EC No. 4.2.99.21
EC Number:5.4.99.5
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
chorismate mutase
Q51507
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
101
11432
Reaction
Chorismate = prephenate
Other sequences found for EC No. 5.4.99.5
General information:
Sequence
0 MKTPEDCTGL ADIREAIDRI DLDIVQALGR RMDYVKAASR FKASEAAIPA PERVAAMLPE
60 RARWAEENGL DAPFVEGLFA QIIHWYIAEQ IKYWRQTRGA A
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
838131
Serino L.,Reimmann C.,Baur H.,Beyeler M.,Visca P.,Haas D.
Structural genes for salicylate biosynthesis from chorismate in Pseudomonas aeruginosa.
Mol. Gen. Genet.
249
217-228
1995
838132
Stover C.K.,Pham X.-Q.T.,Erwin A.L.,Mizoguchi S.D.,Warrener P.,Hickey M.J.,Brinkman F.S.L.,Hufnagle W.O.,Kowalik D.J.,Lagrou M.,Garber R.L.,Goltry L.,Tolentino E.,Westbrock-Wadman S.,Yuan Y.,Brody L.L.,Coulter S.N.,Folger K.R.,Kas A.,Larbig K.,Lim R.M.,Smith K.A.,Spencer D.H.,Wong G.K.-S.,Wu Z.,Paulsen I.T.,Reizer J.,Saier M.H. Jr.,Hancock R.E.W.,Lory S.,Olson M.V.
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.
Nature
406
959-964
2000
838133
Gaille C.,Kast P.,Haas D.
Salicylate biosynthesis in Pseudomonas aeruginosa. Purification and characterization of PchB, a novel bifunctional enzyme displaying isochorismate pyruvate-lyase and chorismate mutase activities.
J. Biol. Chem.
277
21768-21775
2002
838134
DeClue M.S.,Baldridge K.K.,Kuenzler D.E.,Kast P.,Hilvert D.
Isochorismate pyruvate lyase: a pericyclic reaction mechanism?
J. Am. Chem. Soc.
127
15002-15003
2005
838135
Marti S.,Andres J.,Moliner V.,Silla E.,Tunon I.,Bertran J.
Mechanism and plasticity of isochorismate pyruvate lyase: a computational study.
J. Am. Chem. Soc.
131
16156-16161
2009
838136
Zaitseva J.,Lu J.,Olechoski K.L.,Lamb A.L.
Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa.
J. Biol. Chem.
281
33441-33449
2006
838137
Luo Q.,Olucha J.,Lamb A.L.
Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme.
Biochemistry
48
5239-5245
2009
838138
Olucha J.,Ouellette A.N.,Luo Q.,Lamb A.L.
pH Dependence of catalysis by Pseudomonas aeruginosa isochorismate-pyruvate lyase: implications for transition state stabilization and the role of lysine 42.
Biochemistry
50
7198-7207
2011
