Literature DB >> 4590692

Random pathway mechanism involving parallel one- and two- substrate branches for glyoxalase I from yeast.

B Mannervik, T Bartfai, B Górna-Hall.   

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Year:  1974        PMID： 4590692

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  5 in total

1.  Patterns of apparent co-operativity in a simple random non-equilibrium enzyme--substrate--modifier mechanism. Comparison with equilibrium allosteric models.

Authors:  E P Whitehead; M R Egmond
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

2.  A steady-state-kinetic model for formaldehyde dehydrogenase from human liver. A mechanism involving NAD+ and the hemimercaptal adduct of glutathione and formaldehyde as substrates and free glutathione as an allosteric activator of the enzyme.

Authors:  L Uotila; B Mannervik
Journal:  Biochem J       Date:  1979-03-01       Impact factor: 3.857

Review 3.  Nonredox nickel enzymes.

Authors:  Michael J Maroney; Stefano Ciurli
Journal:  Chem Rev       Date:  2013-12-26       Impact factor: 60.622

4.  Probing the active site of glyoxalase I from human erythrocytes by use of the strong reversible inhibitor S-p-bromobenzylglutathione and metal substitutions.

Authors:  A C Aronsson; S Sellin; G Tibbelin; B Mannervik
Journal:  Biochem J       Date:  1981-07-01       Impact factor: 3.857

5.  Comparison of glyoxalase I purified from yeast (Saccharomyces cerevisiae) with the enzyme from mammalian sources.

Authors:  E Marmstål; A C Aronsson; B Mannervik
Journal:  Biochem J       Date:  1979-10-01       Impact factor: 3.857
  5 in total

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