Evidence That Pyridoxal Phosphate Modification of Lysine Residues (Lys-55 and Lys-59) Causes Inactivation of Hydroxymethylbilane Synthase (Porphobilinogen Deaminase)

Biochemical Journal- United Kingdom

doi 10.1042/bj2620119

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August 15, 1989

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Portland Press Ltd.

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Evidence That Pyridoxal Phosphate Modification of Lysine Residues (Lys-55 and Lys-59) Causes Inactivation of Hydroxymethylbilane Synthase (Porphobilinogen Deaminase)

Biochemical Journal- United Kingdom

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Modification of Hydroxymethylbilane Synthase (Porphobilinogen Deaminase) by Pyridoxal 5′-Phosphate. Demonstration of an Essential Lysine Residue

Evidence That the Pyrromethane Cofactor of Hydroxymethylbilane Synthase (Porphobilinogen Deaminase) Is Bound to the Protein Through the Sulphur Atom of Cysteine-242

Structural Insights Into E. Coli Porphobilinogen Deaminase During Synthesis and Exit of 1-Hydroxymethylbilane

Modification of Pig M4lactate Dehydrogenase by Pyridoxal 5'-Phosphate. Demonstration of an Essential Lysine Residue

Anomalous Properties of Lys Residues Buried in Hydrophobic Environments in Proteins

Inactivation of Glutamate Dehydrogenase and Glutamate Synthase fromBacillus Megateriumby Phenylglyoxal, Butane-2,3-Dione and Pyridoxal 5′-Phosphate

Lys Og Varme

Wortmannin Inactivates Phosphoinositide 3-Kinase by Covalent Modification of Lys-802, a Residue Involved in the Phosphate Transfer Reaction.

Orphan Designation: Ile-Ser-Ile-THR-Glu-Ile-Lys-Gly-Val-Ile-Val-His-Arg-Ile-Glu-THR-Ile-Leu-Phe-Lys-Lys-Lys-Lys-Glu-Met-Pro-Ser-Glu-Glu-Gly-Tyr-GLN-Asp, Treatment of Multiple System Atrophy