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
- Functionsdimethylglycine 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
Resource Link UniProtKB ID Q9AGP8 UniProtKB Entry Name DMGO_ARTGO GenBank Gene ID AF329477 - General References
- 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]
- 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]
- 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]
- 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]