Menaquinone-specific prenyl reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
Four genes that encode the homologues of plant geranylgeranyl reductase were isolated from a hyperthermophilic archaeon Archaeoglobus fulgidus, which produces menaquinone with a fully saturated heptaprenyl side chain, menaquinone-7(14H). The recombinant expression of one of the homologues in Escherichia coli led to a distinct change in the quinone profile of the host cells, although the homologue is the most distantly related to the geranylgeranyl reductase. The new compounds found in the profile had successively longer elution times than those of ordinary quinones from E. coli, i.e., menaquinone-8 and ubiquinone-8, in high-performance liquid chromatography on a reversed-phase column. Structural analyses of the new compounds by electron impact-mass spectrometry indicated that their molecular masses progressively increase relative to the ordinary quinones at a rate of 2 U but that they still contain quinone head structures, strongly suggesting that the compounds are quinones with partially saturated prenyl side chains. In vitro assays with dithionite as the reducing agent showed that the prenyl reductase is highly specific for menaquinone-7, rather than ubiquinone-8 and prenyl diphosphates. This novel enzyme noncovalently binds flavin adenine dinucleotide, similar to geranylgeranyl reductase, but was not able to utilize NAD(P)H as the electron donor, unlike the plant homologue.
Hemmi
Hisashi
H
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai, Miyagi 980-8579, Japan. hhemmi@seika.che.tohoku.ac.jp
Takahashi
Yoshihiro
Y
Shibuya
Kyohei
K
Nakayama
Toru
T
Nishino
Tokuzo
T
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019611:Archaeoglobus fulgidus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004227:Dithionite / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism; D013729:Terpenes / Q000737:chemistry / Q000378:metabolism; D024482:Vitamin K 2 / Q000737:chemistry / Q000378:metabolism*
D019843:Archaeal Proteins; D013729:Terpenes; D024482:Vitamin K 2; D004227:Dithionite; D010088:Oxidoreductases; C110920:geranylgeranyl reductase; D010100:Oxygen
Biochim Biophys Acta. 1982 Sep 14;712(3):716-8
7126635
Prog Lipid Res. 1988;27(3):153-75
3151021
J Biol Chem. 1996 Aug 2;271(31):18831-7
8702542
Eur J Biochem. 1998 Jan 15;251(1-2):413-7
9492312
Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12984-8
14566062
J Bacteriol. 1982 Sep;151(3):1397-402
6809730
J Biol Chem. 1999 Jun 18;274(25):18011-6
10364251
Microbiol Rev. 1981 Jun;45(2):316-54
7022156
J Bacteriol. 2004 Jan;186(1):90-7
14679228
FEBS Lett. 1996 Jul 1;389(2):126-30
8766814
J Biol Chem. 1968 Jan 25;243(2):398-407
5635783
Can J Biochem Physiol. 1959 Aug;37(8):911-7
13671378
J Bacteriol. 1999 Dec;181(23):7248-55
10572128
J Am Chem Soc. 1967 Mar 15;89(6):1505-8
6041358
J Bacteriol. 2002 Mar;184(6):1578-86
11872709
Plant Physiol. 1999 Jul;120(3):695-704
10398704