2006
DOI: 10.1016/j.jmb.2006.07.048
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Crystal Structure of Thermus thermophilus Δ1-Pyrroline-5-carboxylate Dehydrogenase

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Cited by 54 publications
(93 citation statements)
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“…These results indicated a predominantly hexameric arrangement. This is consistent with previous structural data describing a hexameric conformation (25), suggesting that TcP5CDH exists as an oligomer. The enzyme bound to mitochondrial membranes exhibited either a hexameric conformation or a protein super-complex arrangement compatible with a dimer of hexamers.…”
Section: Discussionsupporting
confidence: 93%
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“…These results indicated a predominantly hexameric arrangement. This is consistent with previous structural data describing a hexameric conformation (25), suggesting that TcP5CDH exists as an oligomer. The enzyme bound to mitochondrial membranes exhibited either a hexameric conformation or a protein super-complex arrangement compatible with a dimer of hexamers.…”
Section: Discussionsupporting
confidence: 93%
“…1A) and Ser 340 ) enzymes, in which the specific residues are likely to be involved in catalytic processes, as reported previously in archaea and human orthologs (Fig. 1A) (25,66).…”
Section: Identification and In Silico Analysis Of Tcp5cdh-a 1686-bpsupporting
confidence: 76%
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“…UreG functions as a chaperone in the urease active site assembly and is often required to complete the biosynthesis of nickel-enzymes (Zambelli et al, 2009). Pyrroline-5-carboxylate dehydrogenase plays a key role in the metabolic pathway, as it catalyzes the oxidation of proline to glutamate in the presence of NAD (Inagaki et al, 2006;Parsons et al, 2011).…”
Section: Discussionmentioning
confidence: 99%