Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase. (Q53554919)

15 May 2018

title

Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase. (English)

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15 May 2018

author name string

Gregory A Hunter

series ordinal

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15 May 2018

Junshun Zhang

series ordinal

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15 May 2018

Gloria C Ferreira

series ordinal

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15 May 2018

language of work or name

English

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publication date

7 May 2007

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15 May 2018

Journal of Biological Chemistry

published in

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15 May 2018

volume

282

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issue

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15 May 2018

page(s)

23025-23035

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15 May 2018

From cofactor to enzymes. The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes

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Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.

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Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism

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Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor

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Lysine-313 of 5-Aminolevulinate Synthase Acts as a General Base during Formation of the Quinonoid Reaction Intermediates†

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Identifiers

DOI

10.1074/JBC.M609330200

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15 May 2018

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15 May 2018