Mandelate racemase
Details
- Name
- Mandelate racemase
- Synonyms
- 5.1.2.2
- MR
- Gene Name
- mdlA
- Organism
- Pseudomonas putida
- Amino acid sequence
>lcl|BSEQ0011060|Mandelate racemase MSEVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLFAYTPVALK SLKQLLDDMAAMIVNEPLAPVSLEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHE TPLVKLLGANARPVQAYDSHSLDGVKLATERAVTAAELGFRAVKTKIGYPALDQDLAVVR SIRQAVGDDFGIMVDYNQSLDVPAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLN VPVQMGENWLGPEEMFKALSIGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQ EISAHLLAATPTAHWLERLDLAGSVIEPTLTFEGGNAVIPDLPGVGIIWREKEIGKYLV
- Number of residues
- 359
- Molecular Weight
- 38564.39
- Theoretical pI
- 6.04
- GO Classification
- Functionsmandelate racemase activity / metal ion bindingProcessescellular amino acid catabolic process / mandelate catabolic process
- General Function
- Metal ion binding
- Specific Function
- Not Available
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0002973|1080 bp ATGAGTGAAGTACTGATTACCGGCCTGAGGACGCGGGCCGTCAATGTCCCATTGGCCTAC CCCGTTCACACCGCTGTTGGAACTGTTGGCACAGCGCCTCTTGTTCTGATCGACCTGGCC ACCAGTGCCGGCGTGGTAGGCCATTCCTACCTGTTCGCATACACCCCCGTTGCGTTGAAG TCGCTGAAGCAGCTCCTGGACGACATGGCAGCCATGATCGTCAACGAACCATTGGCACCG GTTAGCTTGGAAGCCATGCTCGCAAAACGCTTCTGCCTGGCAGGTTATACGGGATTGATC CGAATGGCCGCTGCTGGCATCGATATGGCAGCTTGGGATGCGCTGGGCAAGGTTCACGAA ACGCCACTAGTAAAACTCCTCGGCGCGAACGCTCGACCAGTTCAGGCTTATGACAGCCAC AGCTTGGATGGAGTCAAACTCGCGACTGAGCGCGCTGTGACCGCAGCAGAACTCGGATTC CGGGCGGTTAAGACCAAGATCGGCTATCCGGCATTGGATCAAGATCTGGCAGTCGTGCGC AGCATACGCCAAGCAGTAGGTGACGACTTCGGCATCATGGTCGACTACAACCAGAGTTTG GATGTACCAGCCGCAATCAAACGCAGCCAGGCGCTGCAGCAAGAGGGCGTCACCTGGATT GAAGAGCCGACGCTTCAACACGATTACGAAGGCCATCAGCGCATTCAAAGCAAGCTCAAT GTGCCCGTCCAGATGGGTGAGAACTGGCTCGGCCCTGAGGAGATGTTCAAAGCATTGAGC ATCGGTGCATGCCGGTTGGCTATGCCAGATGCAATGAAGATCGGTGGCGTGACGGGCTGG ATCCGAGCCAGTGCACTCGCACAACAATTCGGTATTCCAATGTCCAGCCACCTGTTCCAA GAAATCAGCGCTCACCTGCTAGCCGCCACCCCAACTGCGCATTGGCTGGAGCGTTTGGAT CTCGCCGGCAGCGTCATCGAGCCTACTCTTACATTTGAGGGCGGAAATGCTGTGATTCCG GATCTCCCTGGCGTTGGGATCATCTGGCGCGAGAAAGAAATCGGGAAATATCTGGTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P11444 UniProtKB Entry Name MANR_PSEPU GenBank Protein ID 151352 GenBank Gene ID M19043 - General References
- Ransom SC, Gerlt JA, Powers VM, Kenyon GL: Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida. Biochemistry. 1988 Jan 26;27(2):540-5. [Article]
- Tsou AY, Ransom SC, Gerlt JA, Buechter DD, Babbitt PC, Kenyon GL: Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry. 1990 Oct 23;29(42):9856-62. [Article]
- Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA: Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature. 1990 Oct 18;347(6294):692-4. [Article]
- Landro JA, Kallarakal AT, Ransom SC, Gerlt JA, Kozarich JW, Neidhart DJ, Kenyon GL: Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant. Biochemistry. 1991 Sep 24;30(38):9274-81. [Article]
- Neidhart DJ, Howell PL, Petsko GA, Powers VM, Li RS, Kenyon GL, Gerlt JA: Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues. Biochemistry. 1991 Sep 24;30(38):9264-73. [Article]
- Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL: Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317. Biochemistry. 1995 Mar 7;34(9):2777-87. [Article]
- Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL: Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant. Biochemistry. 1995 Mar 7;34(9):2788-97. [Article]