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Items: 1 to 20 of 105

1.

Bradyrhizobium japonicum porphobilinogen synthase uses two Mg(II) and monovalent cations.

Petrovich RM, Litwin S, Jaffe EK.

J Biol Chem. 1996 Apr 12;271(15):8692-9.

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Pseudomonas aeruginosa contains a novel type V porphobilinogen synthase with no required catalytic metal ions.

Frankenberg N, Jahn D, Jaffe EK.

Biochemistry. 1999 Oct 19;38(42):13976-82.

PMID:
10529244
5.

Rhodobacter capsulatus porphobilinogen synthase, a high activity metal ion independent hexamer.

Bollivar DW, Clauson C, Lighthall R, Forbes S, Kokona B, Fairman R, Kundrat L, Jaffe EK.

BMC Biochem. 2004 Nov 22;5:17.

6.

Characterization of the role of the stimulatory magnesium of Escherichia coli porphobilinogen synthase.

Jaffe EK, Ali S, Mitchell LW, Taylor KM, Volin M, Markham GD.

Biochemistry. 1995 Jan 10;34(1):244-51.

PMID:
7819203
7.

Porphobilinogen synthase from Escherichia coli is a Zn(II) metalloenzyme stimulated by Mg(II).

Mitchell LW, Jaffe EK.

Arch Biochem Biophys. 1993 Jan;300(1):169-77.

PMID:
8424649
8.

Mechanistic basis for suicide inactivation of porphobilinogen synthase by 4,7-dioxosebacic acid, an inhibitor that shows dramatic species selectivity.

Kervinen J, Jaffe EK, Stauffer F, Neier R, Wlodawer A, Zdanov A.

Biochemistry. 2001 Jul 27;40(28):8227-36.

PMID:
11444968
9.

The molecular mechanism of lead inhibition of human porphobilinogen synthase.

Jaffe EK, Martins J, Li J, Kervinen J, Dunbrack RL Jr.

J Biol Chem. 2001 Jan 12;276(2):1531-7.

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Tracking the evolution of porphobilinogen synthase metal dependence in vitro.

Frère F, Reents H, Schubert WD, Heinz DW, Jahn D.

J Mol Biol. 2005 Feb 4;345(5):1059-70. Epub 2004 Dec 21.

PMID:
15644204
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The porphobilinogen synthase family of metalloenzymes.

Jaffe EK.

Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):115-28. Review.

PMID:
10666591
14.

Investigations on the metal switch region of human porphobilinogen synthase.

Jaffe EK.

J Biol Inorg Chem. 2003 Jan;8(1-2):176-84. Epub 2002 Sep 28.

PMID:
12459913
16.

Porphobilinogen synthase, the first source of heme's asymmetry.

Jaffe EK.

J Bioenerg Biomembr. 1995 Apr;27(2):169-79. Review.

PMID:
7592564
17.

Mechanistic implications of mutations to the active site lysine of porphobilinogen synthase.

Mitchell LW, Volin M, Martins J, Jaffe EK.

J Biol Chem. 2001 Jan 12;276(2):1538-44.

18.

Porphobilinogen synthase from pea: expression from an artificial gene, kinetic characterization, and novel implications for subunit interactions.

Kervinen J, Dunbrack RL Jr, Litwin S, Martins J, Scarrow RC, Volin M, Yeung AT, Yoon E, Jaffe EK.

Biochemistry. 2000 Aug 1;39(30):9018-29.

PMID:
10913315
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