Comparative characterisation of thiamin diphosphate-dependent decarboxylases

被引:43
|
作者
Gocke, Doerte [1 ]
Graf, Thorsten [1 ]
Brosi, Helen [1 ]
Frindi-Wosch, Ilona [1 ]
Walter, Lydia [2 ]
Mueller, Michael [2 ]
Pohl, Martina [1 ]
机构
[1] Univ Dusseldorf, Res Ctr Julich, Inst Mol Enzyme Technol, D-52426 Julich, Germany
[2] Univ Freiburg, Inst Pharmaceut Sci, D-79104 Freiburg, Germany
关键词
Enzymatic decarboxylation; Enzymatic carboligation; 2-Hydroxy ketones; Phenylacetylcarbinol; Acetoin; KETO ACID DECARBOXYLASE; C BOND FORMATION; PYRUVATE DECARBOXYLASE; ZYMOMONAS-MOBILIS; BENZOYLFORMATE DECARBOXYLASE; BENZALDEHYDE LYASE; ENANTIOSELECTIVE SYNTHESIS; SUBSTRATE-SPECIFICITY; ENZYMATIC-REACTIONS; PSEUDOMONAS-PUTIDA;
D O I
10.1016/j.molcatb.2009.03.019
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Several 2-keto acid decarboxylases catalyse an acyloin condensation-like carboligase reaction beside their physiological decarboxylase activity. Although many data concerning stability and catalytic potential of these enzymes are available, a standard evaluation under similar reaction conditions is lacking. In this comprehensive survey we assemble already published data combined with new studies of three bacterial pyruvate decarboxylases, yeast pyruvate decarboxylase, benzoylformate decarboxylase from Pseudomonas putida (BFD) and the branched-chain 2-keto acid decarboxylase from Lactococcus lactis (KdcA). The obtained results proof that the optima for activity and stability are rather similar if comparable reaction conditions are used. Although the substrate ranges of the decarboxylase reaction of the various pyruvate decarboxylases are similar as well, they differ remarkably from those of BFD and KdcA. We further show that the range of acceptable donor aldehydes for the carboligase reaction of a respective enzyme can be reliably predicted from the substrate range of decarboxylase reaction. (C) 2009 Elsevier B.V. All rights reserved.
引用
收藏
页码:30 / 35
页数:6
相关论文
共 50 条
  • [1] Substrate specificity in thiamin diphosphate-dependent decarboxylases
    Andrews, Forest H.
    McLeish, Michael J.
    BIOORGANIC CHEMISTRY, 2012, 43 : 26 - 36
  • [2] Use of thiamin diphosphate-dependent decarboxylases in chiral synthesis of carboligase products
    Baykal, AT
    Chakraborty, S
    Nemeria, N
    Jordan, F
    FASEB JOURNAL, 2006, 20 (04): : A40 - A40
  • [3] Synthetic potential of thiamin diphosphate-dependent enzymes
    Sprenger, GA
    Pohl, M
    JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 1999, 6 (03) : 145 - 159
  • [4] Frontiers in the enzymology of thiamin diphosphate-dependent enzymes
    Prajapati, Sabin
    Pappenheim, Fabian Rabe von
    Tittmann, Kai
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 2022, 76
  • [5] Synthesis with good enantiomeric excess of both enantiomers of α-ketols and acetolactates by two thiamin diphosphate-dependent decarboxylases
    Baykal, Ahmet
    Chakraborty, Surnit
    Dodoo, Afua
    Jordan, Frank
    BIOORGANIC CHEMISTRY, 2006, 34 (06) : 380 - 393
  • [6] Regulation of thiamin diphosphate-dependent 2-oxo acid decarboxylases by substrate and thiamin diphosphate.Mg(II) - evidence for tertiary and quaternary interactions
    Jordan, F
    Nemeria, N
    Guo, FS
    Baburina, I
    Gao, YH
    Kahyaoglu, A
    Li, HJ
    Wang, J
    Yi, JZ
    Guest, JR
    Furey, W
    BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1998, 1385 (02): : 287 - 306
  • [7] A standard numbering scheme for thiamine diphosphate-dependent decarboxylases
    Vogel, Constantin
    Widmann, Michael
    Pohl, Martina
    Pleiss, Juergen
    BMC BIOCHEMISTRY, 2012, 13
  • [8] Remarkable stabilization of zwitterionic intermediates may account for a billion-fold rate acceleration by thiamin diphosphate-dependent decarboxylases
    Jordan, F
    Li, HJ
    Brown, A
    BIOCHEMISTRY, 1999, 38 (20) : 6369 - 6373
  • [9] Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate-dependent enzymes for asymmetric chemoenzymatic synthesis
    Mueller, Michael
    Gocke, Doerte
    Pohl, Martina
    FEBS JOURNAL, 2009, 276 (11) : 2894 - 2904
  • [10] Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase
    Yep, Alejandra
    Kenyon, George L.
    McLeish, Michael J.
    BIOORGANIC CHEMISTRY, 2006, 34 (06) : 325 - 336