Dimethylglycine oxidase

Details

Name
Dimethylglycine oxidase
Synonyms
  • 1.5.3.10
  • DMGO
Gene Name
dmg
Organism
Arthrobacter globiformis
Amino acid sequence
>lcl|BSEQ0012081|Dimethylglycine oxidase
MASTPRIVIIGAGIVGTNLADELVTRGWNNITVLDQGPLNMPGGSTSHAPGLVFQTNPSK
TMASFAKYTVEKLLSLTEDGVSCFNQVGGLEVATTETRLADLKRKLGYAAAWGIEGRLLS
PAECQELYPLLDGENILGGLHVPSDGLASAARAVQLLIKRTESAGVTYRGSTTVTGIEQS
GGRVTGVQTADGVIPADIVVSCAGFWGAKIGAMIGMAVPLLPLAHQYVKTTPVPAQQGRN
DQPNGARLPILRHQDQDLYYREHGDRYGIGSYAHRPMPVDVDTLGAYAPETVSEHHMPSR
LDFTLEDFLPAWEATKQLLPALADSEIEDGFNGIFSFTPDGGPLLGESKELDGFYVAEAV
WVTHSAGVAKAMAELLTTGRSETDLGECDITRFEDVQLTPEYVSETSQQNFVEIYDVLHP
LQPRLSPRNLRVSPFHARHKELGAFFLEAGGWERPYWFEANAALLKEMPAEWLPPARDAW
SGMFSSPIAAAEAWKTRTAVAMYDMTPLKRLEVSGPGALKLLQELTTADLAKKPGAVTYT
LLLDHAGGVRSDITVARLSEDTFQLGANGNIDTAYFERAARHQTQSGSATDWVQVRDTTG
GTCCIGLWGPLARDLVSKVSDDDFTNDGLKYFRAKNVVIGGIPVTAMRLSYVGELGWELY
TSADNGQRLWDALWQAGQPFGVIAAGRAAFSSLRLEKGYRSWGTDMTTEHDPFEAGLGFA
VKMAKESFIGKGALEGRTEEASARRLRCLTIDDGRSIVLGKEPVFYKEQAVGYVTSAAYG
YTVAKPIAYSYLPGTVSVGDSVDIEYFGRRITATVTEDPLYDPKMTRLRG
Number of residues
830
Molecular Weight
89983.935
Theoretical pI
5.0
GO Classification
Functions
dimethylglycine oxidase activity / nucleotide binding
General Function
Nucleotide binding
Specific Function
Catalyzes the oxidative demethylation of N,N-dimethylglycine to yield sarcosine, formaldehyde and hydrogen peroxide. The oxidation of dimethylglycine is coupled to the synthesis of 5,10-methylenetetrahydrofolate through an unusual substrate channeling mechanism. This channeling occurs by nonbiased diffusion of the iminium intermediate through a large solvent cavity connecting active site 1 (N-terminus) and active site 2 (C-terminus). The synthesis of 5,10-methylenetetrahydrofolate (at active site 2) prevents the accumulation of formaldehyde, formed by hydrolysis of the iminium intermediate product (at active site 1). Does not oxidize sarcosine.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0005786|2493 bp
ATGGCATCGACGCCGCGTATTGTCATTATTGGAGCCGGCATTGTCGGTACGAACCTGGCC
GACGAGCTGGTCACCCGGGGCTGGAATAACATCACTGTCCTGGACCAGGGGCCTTTGAAT
ATGCCCGGCGGGTCCACGTCCCATGCCCCGGGCCTGGTTTTCCAGACCAACCCGTCCAAG
ACCATGGCCTCTTTCGCCAAGTACACGGTGGAGAAGCTGCTGTCGCTGACCGAGGACGGG
GTGAGCTGCTTCAACCAGGTCGGTGGCCTGGAAGTGGCCACCACCGAAACCCGCCTCGCT
GACCTGAAGCGCAAACTCGGCTACGCCGCCGCCTGGGGCATCGAAGGGCGCCTCCTGTCC
CCGGCCGAGTGCCAGGAGCTGTACCCGCTCCTGGACGGGGAAAACATCCTGGGCGGCCTC
CACGTGCCCAGCGATGGCCTGGCCAGCGCCGCCCGTGCGGTGCAGCTGCTGATCAAACGC
ACCGAGTCCGCCGGGGTCACATACCGCGGTTCGACCACCGTGACGGGCATTGAGCAGTCC
GGAGGCCGTGTCACGGGCGTGCAGACCGCCGACGGCGTGATCCCGGCCGATATCGTGGTG
TCCTGCGCCGGGTTCTGGGGCGCGAAGATCGGGGCCATGATCGGCATGGCCGTTCCCCTG
CTCCCGCTGGCCCACCAGTACGTAAAAACCACCCCGGTACCGGCGCAGCAGGGCAGGAAC
GACCAGCCGAACGGGGCCCGGCTGCCGATCCTGCGCCACCAGGACCAGGACCTCTACTAC
CGCGAACACGGGGACCGGTACGGCATCGGCTCCTACGCCCACCGGCCCATGCCCGTGGAC
GTCGACACCCTGGGGGCCTACGCGCCCGAGACCGTCAGCGAACACCACATGCCCTCCCGC
CTCGACTTCACCCTGGAGGACTTCCTGCCGGCGTGGGAGGCCACCAAGCAGCTCCTGCCC
GCGCTGGCGGACAGCGAGATCGAGGACGGCTTCAACGGCATCTTCTCCTTCACCCCCGAC
GGCGGGCCGCTCCTTGGCGAATCCAAGGAACTCGACGGCTTCTACGTCGCCGAAGCCGTC
TGGGTCACGCACTCCGCCGGCGTGGCCAAGGCCATGGCCGAACTGCTGACCACCGGCCGG
TCCGAGACCGACCTGGGCGAGTGCGACATCACCCGCTTCGAGGACGTCCAGCTCACCCCC
GAATACGTCAGCGAAACCTCACAGCAGAACTTCGTGGAAATCTACGACGTCCTGCACCCG
CTCCAGCCCAGACTCTCCCCCCGCAACCTGCGCGTGAGCCCCTTCCACGCCCGGCACAAA
GAACTCGGCGCGTTCTTCCTGGAAGCCGGCGGCTGGGAACGGCCCTACTGGTTCGAAGCC
AACGCCGCACTCCTCAAGGAGATGCCGGCCGAGTGGCTGCCGCCCGCACGCGACGCCTGG
TCCGGAATGTTCAGCTCCCCGATCGCCGCCGCCGAAGCCTGGAAAACCCGCACGGCCGTA
GCCATGTACGACATGACCCCGCTCAAGCGCCTCGAGGTCTCCGGCCCGGGGGCCCTCAAG
CTCCTGCAGGAACTGACGACGGCGGACCTGGCCAAGAAGCCGGGCGCGGTCACCTACACC
CTGCTGCTCGACCACGCCGGCGGCGTGCGAAGCGACATCACGGTGGCCCGCCTGAGCGAG
GACACCTTCCAGCTCGGCGCCAACGGCAACATCGACACCGCCTACTTCGAGCGGGCGGCC
CGGCACCAGACGCAAAGCGGATCCGCCACCGACTGGGTCCAGGTGCGCGACACCACCGGC
GGCACCTGCTGCATCGGCCTCTGGGGCCCGCTCGCCCGGGACCTCGTCAGCAAAGTCAGC
GACGACGACTTCACCAACGACGGCCTGAAGTACTTCCGGGCCAAGAACGTCGTCATCGGC
GGCATTCCCGTTACCGCCATGCGGCTTTCCTACGTCGGTGAACTCGGCTGGGAGCTGTAC
ACCAGCGCCGACAACGGACAGCGGCTGTGGGATGCGCTCTGGCAGGCAGGACAGCCCTTC
GGAGTCATCGCCGCCGGACGCGCGGCATTCAGCTCCCTGCGGCTCGAAAAGGGCTACCGC
TCCTGGGGAACCGACATGACCACGGAGCACGACCCCTTCGAAGCAGGGCTCGGATTCGCC
GTCAAGATGGCCAAGGAGAGCTTCATCGGCAAGGGCGCGCTCGAAGGCCGGACCGAAGAG
GCCTCCGCCCGCCGGCTGCGCTGCCTGACCATCGACGACGGCCGGTCCATCGTCCTCGGC
AAGGAACCCGTCTTCTACAAGGAACAGGCCGTCGGCTACGTCACCAGCGCCGCCTACGGG
TACACCGTGGCCAAACCCATCGCCTACTCCTACCTGCCGGGCACCGTCTCGGTCGGCGAC
TCCGTCGACATCGAATACTTCGGACGGCGCATCACCGCCACCGTCACAGAAGACCCGCTG
TACGACCCGAAAATGACCAGGCTCCGCGGCTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDQ9AGP8
UniProtKB Entry NameDMGO_ARTGO
GenBank Gene IDAF329477
General References
  1. Meskys R, Harris RJ, Casaite V, Basran J, Scrutton NS: Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism. Eur J Biochem. 2001 Jun;268(12):3390-8. [Article]
  2. Basran J, Bhanji N, Basran A, Nietlispach D, Mistry S, Meskys R, Scrutton NS: Mechanistic aspects of the covalent flavoprotein dimethylglycine oxidase of Arthrobacter globiformis studied by stopped-flow spectrophotometry. Biochemistry. 2002 Apr 9;41(14):4733-43. [Article]
  3. Leys D, Basran J, Scrutton NS: Channelling and formation of 'active' formaldehyde in dimethylglycine oxidase. EMBO J. 2003 Aug 15;22(16):4038-48. [Article]
  4. Tralau T, Lafite P, Levy C, Combe JP, Scrutton NS, Leys D: An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J Biol Chem. 2009 Jun 26;284(26):17826-34. doi: 10.1074/jbc.M109.006262. Epub 2009 Apr 15. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB03256(6R)-Folinic acidexperimentalunknownDetails