Methylaspartate ammonia-lyase
Details
- Name
- Methylaspartate ammonia-lyase
- Synonyms
- 3-methylaspartase ammonia-lyase
- 4.3.1.2
- Beta-methylaspartase
- MAL
- Gene Name
- Not Available
- Organism
- Clostridium tetanomorphum
- Amino acid sequence
>lcl|BSEQ0019330|Methylaspartate ammonia-lyase MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLE DGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMT VNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDN VDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVY GTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGV DAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKANGMGAYCGGT CNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRRK
- Number of residues
- 413
- Molecular Weight
- 45533.9
- Theoretical pI
- 5.13
- GO Classification
- Functionscobalamin binding / metal ion binding / methylaspartate ammonia-lyase activityProcessesglutamate catabolic process via L-citramalate
- General Function
- Methylaspartate ammonia-lyase activity
- Specific Function
- Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-methylaspartate), L-aspartate, fumarate and ethylfumarate as substrates.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0005408|1242 bp ATGAAAATTGTTGACGTACTTTGTACACCAGGATTAACTGGATTCTATTTTGATGACCAA AGAGCAATCAAAAAGGGAGCAGGACATGATGGATTTACATATACTGGCTCTACTGTAACA GAAGGATTTACTCAAGTAAGACAAAAAGGTGAATCAATATCTGTATTATTAGTTCTTGAA GATGGTCAGGTTGCTCACGGAGATTGTGCTGCAGTTCAGTACTCAGGAGCAGGCGGAAGA GATCCATTATTCTTAGCTAAAGATTTTATACCTGTTATAGAAAAAGAAATAGCTCCAAAA TTGATTGGAAGAGAAATAACTAACTTTAAACCAATGGCAGAAGAATTCGACAAAATGACT GTAAATGGTAATAGATTACATACTGCTATCAGATATGGTATAACTCAGGCTATACTTGAT GCAGTAGCTAAAACTAGAAAAGTAACTATGGCTGAAGTAATCAGAGATGAATACAATCCA GGAGCAGAAATCAATGCAGTTCCTGTATTTGCTCAGTCAGGTGATGATAGATACGATAAC GTTGATAAGATGATAATTAAAGAAGCTGATGTTTTACCACATGCTTTAATCAACAATGTT GAAGAAAAATTAGGACTTAAAGGAGAAAAACTTCTTGAGTACGTTAAATGGTTAAGAGAT AGAATAATCAAATTAAGAGTAAGAGAAGACTATGCTCCAATATTCCACATCGACGTATAT GGAACAATCGGTGCTGCATTTGATGTTGACATCAAGGCTATGGCTGATTACATTCAGACT TTAGCTGAAGCTGCTAAGCCATTCCACTTAAGAATTGAAGGACCAATGGACGTTGAAGAT AGACAAAAACAAATGGAAGCTATGAGAGACTTAAGAGCTGAATTAGACGGAAGAGGAGTA GACGCAGAATTAGTTGCTGATGAATGGTGTAATACAGTTGAAGATGTTAAATTCTTCACT GATAACAAAGCTGGACACATGGTTCAGATCAAAACTCCAGACCTTGGTGGAGTTAACAAT ATAGCAGATGCTATTATGTACTGTAAAGCTAACGGAATGGGAGCTTATTGTGGAGGAACT TGTAACGAAACTAACAGATCCGCTGAAGTTACAACTAACATAGGTATGGCTTGTGGAGCT AGACAGGTTCTTGCTAAACCAGGTATGGGTGTTGACGAAGGAATGATGATCGTTAAGAAC GAAATGAACAGAGTTTTAGCTCTTGTAGGAAGAAGAAAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q05514 UniProtKB Entry Name MAAL_CLOTT GenBank Gene ID S48141 - General References
- Goda SK, Minton NP, Botting NP, Gani D: Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. Biochemistry. 1992 Nov 10;31(44):10747-56. [Article]
- Brecht M, Kellermann J, Pluckthun A: Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. FEBS Lett. 1993 Mar 15;319(1-2):84-9. [Article]
- Holloway DE, Marsh EN: Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes. FEBS Lett. 1993 Feb 8;317(1-2):44-8. [Article]
- Marsh EN, Holloway DE: Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes. FEBS Lett. 1992 Sep 28;310(2):167-70. [Article]
- BARKER HA, SMYTH RD, WILSON RM, WEISSBACH H: The purification and properties of beta-methylaspartase. J Biol Chem. 1959 Feb;234(2):320-8. [Article]
- Raj H, Weiner B, Veetil VP, Reis CR, Quax WJ, Janssen DB, Feringa BL, Poelarends GJ: Alteration of the diastereoselectivity of 3-methylaspartate ammonia lyase by using structure-based mutagenesis. Chembiochem. 2009 Sep 4;10(13):2236-45. doi: 10.1002/cbic.200900311. [Article]
- Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH: The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J Biol Chem. 2002 Mar 8;277(10):8306-11. Epub 2001 Dec 17. [Article]
- Raj H, Szymanski W, de Villiers J, Rozeboom HJ, Veetil VP, Reis CR, de Villiers M, Dekker FJ, de Wildeman S, Quax WJ, Thunnissen AM, Feringa BL, Janssen DB, Poelarends GJ: Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids. Nat Chem. 2012 Apr 29;4(6):478-84. doi: 10.1038/nchem.1338. [Article]