1.5.5.2 D370A mutant form of PutA86-601. The ratio of turnover-number to Km-value is 2.8fold lower than the ratio of the wild-type PutA86-601 658211 1.5.5.2 D370A/Y540F mutant form of PutA86-601. The ratio of turnover-number to Km-value is 15fold lower than the ratio of the wild-type PutA86-601 658211 1.5.5.2 F10E/L12E construction of a variant with a more polar N-terminus, mutant F10E/L12E, because Thermus thermophilus ProDH (TtProDH), produced through fusion with maltose-binding protein (MBP) appears to be prone to aggregation. Preparation of TtProDH mutant variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, the mutant shows no electron density for an AMP moiety of the cofactor -, 743834 1.5.5.2 K110A inactive 724389 1.5.5.2 L432P mutant form of PutA86-669, 5fold decrease in turnover-number and a severe loss in thermostability 658033 1.5.5.2 additional information expression of PRODH/POX in DLD-1 colorectal cancer cells significantly decreases basal and maximal respiration at both 3 and 5 days, and proline addition exacerbates this effect. PRODH/POX-dependent inhibition of respiration can be modulated by the duration of PRODH/POX expression and the availability of proline 741588 1.5.5.2 additional information generation of an enzyme-deficient prodh1 mutant 741858 1.5.5.2 additional information mutants deficient in proline dehydrogenase activity 392572 1.5.5.2 additional information the truncated form of Pseudomonas putida PutA shows proline dehydrogenase activity -, 742641 1.5.5.2 additional information truncated enzyme containing residues 86-601 and only four Trp residues. Substantial conformational changes of truncated protein upon addition of proline 671977 1.5.5.2 W194F mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 50% 671977 1.5.5.2 W194F/W211F mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 95% 671977 1.5.5.2 W211F mutation in truncated enzyme containing residues 86-601, ratio of kcat to Km-value drops by 80% 671977 1.5.5.2 Y203F the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme 724389 1.5.5.2 Y540A a construct consisting of residue 86-630 of PutA is used 696361 1.5.5.2 Y540F mutant form of PutA86-601. The ratio of turnover-number to Km-value is 5.8fold lower than the ratio of the wild-type PutA86-601 658211 1.5.5.2 Y540S a construct consisting of residue 86-630 of PutA is used 696361