TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 14 November 1997
Last modified: 12 October 1998


Molybdopterin­containing proteins

All mononuclear molybdenum (Mo) and tungsten (W) proteins possess a pterin cofactor that coordinates to the metal atom via its dithiolene group. The pterin cofactor common to Mo­ and W­containing enzymes is frequently referred to by the trivial name molybdopterin, but this term refers to the metal­free organic cofactor alone [1, 2]. For historical reasons, there are inconsistencies in the terminology used to designate the metal­bound molybdopterin [3]; we use the term molybdenum cofactor (Moco) for both Mo­ and W­bound molybdopterin. In eukaryotic enzymes the molybdopterin exists in the mononucleotide form (R = H), whereas in enzymes from prokaryota it can be found as the dinucleotide of adenine, cytosine, guanine or hypoxanthine (R = AMP, CMP, GMP or HMP).

Molybdopterin­containing proteins can be classified according to their biological function, by molybdopterin centre type, by type and number of prosthetic centres, and by sequence similarity.

Biosynthesis of molybdopterin in metabolic pathway databases

KEGG PUMA Boehringer
Mannheim
map
EcoCyc
MAP00790; Folate biosynthesis
-
K1 L1 Folic acid biosynthesis
K2 L2

Molybdopterin­containing proteins by function

Function Protein class
Catalysis Oxidoreductases
  • Aldehyde ferredoxin oxidoreductase
  • Aldehyde oxidase
  • Arsenite oxidase
  • Carboxylic acid reductase
  • CO dehydrogenase
  • DMSO reductase
  • Formaldehyde ferredoxin oxidoreductase
  • Formate dehydrogenase
  • Formylmethanofuran dehydrogenase
  • Glyceraldehyde­3­phosphate ferredoxin oxidoreductase
  • Nitrate reductases
  • Polysulphide reductase
  • Sulphite oxidase
  • Trimethylamine N­oxide reductase
  • Xanthine oxidase
  • Xanthine dehydrogenase

Molybdopterin­containing proteins by molybdopterin centre type

Molybdopterin centre Protein family
Mo or W cofactor image

M·molybdopterin cofactor (M = Mo or W; R = H or CMP)
Mo or W cofactor image

M·2 molybdopterin (M = Mo or W; R = H, AMP, GMP, HMP)

Molybdopterin­containing proteins by type and number of prosthetic centres

Molybdopterin­containing proteins
Simple Complex

Molybdopterin­containing proteins in motif databases

PRINTS ID PRINTS AC PROSITE/BLOCKS ID PROSITE AC BLOCKS AC
EUMOPTERIN PR00407 MOLYBDOPTERIN_EUK PS00559 BL00559
-
-
MOLYBDOPTERIN_PROK_1
MOLYBDOPTERIN_PROK_2
MOLYBDOPTERIN_PROK_3
PS00551
PS00490
PS00932
BL00551

Molybdopterin­containing proteins in PROMISE

PROMISE ID Description
AOR Aldehyde ferredoxin oxidoreductase family (including aldehyde ferredoxin oxidoreductase, formaldehyde ferredoxin oxidoreductase, glyceraldehyde­3­phosphate ferredoxin oxidoreductase, carboxylic acid reductase and hydroxycarboxylate viologen oxidoreductase)
SULFOXIDASE Sulphite oxidase family (including sulphite oxidase and plant and fungal assimilatory nitrate reductases)
DMSOR DMSO reductase family (including DMSO reductase, dissimilatory nitrate reductases, formylmethanofuran dehydrogenase, trimethylamine N­oxide reductase, arsenite oxidase, formate dehydrogenase and polysulphide reductase)
XANTOXIDASE Xanthine oxidase family (including xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, CO dehydrogenase)

HET groups in PDB (at BSM)

HET group Description Formula HET group Description Formula
4MO
Molybdenum(IV) ion Mo4+
6MO
Molybdenum(VI) ion Mo6+
MO
Molybdenum ion Mo4+/6+
MCN
Molybdopterin cytosine dinucleotide C19H22N8O13P2S2
MGD
Molybdopterin guanine dinucleotide C20H24N10O13P2S2
MTE
Molybdopterin C10H14N5O6PS2
PTE
Tungstopterin cofactor C20H29N10O14MgP2S4W

Molybdopterin­containing proteins in 3­D databases

Prosthetic centre Enzymes
Moco
  • DMSO reductase
  • Moco-Fe2S2
  • Xanthine oxidase family
  • Moco-Fe4S4/Fe3S4
  • Aldehyde ferredoxin oxidoreductase
  • DMSO reductase family
  • Moco-haem
  • Sulphite oxidase family
  • References

    1. Hille, R. (1996a) Structure and function of mononuclear molybdenum enzymes. J. Biol. Inorg. Chem. 1, 397-404.
    2. Hille, R. (1996b) The mononuclear molybdenum enzymes. Chem. Rev. 96, 2757-2816.
    3. Kisker, C., Schindelin, H. and Rees, D.C. (1997) Molybdenum­cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 66, 233-267.
    4. Nomenclature Committee of the International Union of Biochemistry (NC-IUB) (1991) Nomenclature of electron­transfer proteins. Recommendations 1989. Eur. J. Biochem. 200, 599-611.
    General references on molybdopterin­containing proteins