Literature DB >> 4817560

Subunit interactions in enzyme catalysis. Kinetic analysis of subunit interactions in the enzyme L-phenylalanine ammonia-lyase.

J Nari, C Mouttet, F Fouchier, J Ricard.   

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Year:  1974        PMID： 4817560     DOI： 10.1111/j.1432-1033.1974.tb03291.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


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  5 in total

1.  Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms.

Authors:  E P Whitehead
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

2.  Microbial L-phenylalanine ammonia-lyase. Purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani.

Authors:  K K Kalghatgi; P V Subba Rao
Journal:  Biochem J       Date:  1975-07       Impact factor: 3.857

3.  Ionic control of immobilized enzymes. Kinetics of acid phosphatase bound to plant cell walls.

Authors:  J Ricard; G Noat; M Crasnier; D Job
Journal:  Biochem J       Date:  1981-05-01       Impact factor: 3.857

4.  Phenylalanine Ammonia-Lyase from Tomato Cell Cultures Inoculated with Verticillium albo-atrum.

Authors:  M A Bernards; B E Ellis
Journal:  Plant Physiol       Date:  1991-12       Impact factor: 8.340

5.  Fungal and Plant Phenylalanine Ammonia-lyase.

Authors:  Min Woo Hyun; Yeo Hong Yun; Jun Young Kim; Seong Hwan Kim
Journal:  Mycobiology       Date:  2011-12-07       Impact factor: 1.858
  5 in total

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