Enzymatic synthesis of dihydrosirohydrochlorin (precorrin‐2) and of a novel pyrrocorphin by uroporphyrinogen III methylase

FEBS Letters

Warren, Martin J.²  Scott, A.Ian²  Sowa, Blair A.¹  Roessner, Charles A.²  Santander, Patricio J.²  Stolowich, Neal J.² 

[1] Centre for Biological N M R, Department of Veterinary Pathology, Texas A & M University, College Station, TX 77843, USA;Centre for Biological N M R, Department of Chemistry, Texas A & M University, College Station, TX 77843, USA

关键词: Uroporphyrinogen III methylase;    Dihydrosirohydrochlorin;    Precorrin-2;    Dipyrrocorphin;    Pyrrocorphin;    NMR;    13C-;    uro'gen;    uroporphyrinogen;    SAM;    S-adenosyl methionine;    SUMT;    S-adenosyl methionine uroporphyrinogen methyl transferase;    NMR;    nuclear magnetic resonance;    HPLC;    high pressure liquid chromatography;    pbg;    porphobilinogen;   

DOI  :  10.1016/0014-5793(90)80640-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Uroporphyrinogen III methylase was purified from a recombinant hemB⁻ strain of E. coli harbouring a plasmid containing the cysG gene. N-terminal analysis of this purified protein gave an amino acid sequence corresponding to that predicted from the genetic code. From the u.v./visible spectrum of the reaction catalysed by this SAM dependent methylase it was possible to observe the sequential appearance of the chromophores of a dipyrrocorphin and subsequently of a pyrrocorphin. Confirmation of this transformation was obtained from ¹³C-NMR studies when it was demonstrated, for the first time directly, that uroporphyrinogen is initially converted into dihydrosirohydrochlorin (precorrin-2) and then, by further methylation, into a novel trimethylpyrrocorphin.

【 授权许可】

Unknown