2014
DOI: 10.1371/journal.pone.0113212
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Structure of Putrescine Aminotransferase from Escherichia coli Provides Insights into the Substrate Specificity among Class III Aminotransferases

Abstract: YgjG is a putrescine aminotransferase enzyme that transfers amino groups from compounds with terminal primary amines to compounds with an aldehyde group using pyridoxal-5′-phosphate (PLP) as a cofactor. Previous biochemical data show that the enzyme prefers primary diamines, such as putrescine, over ornithine as a substrate. To better understand the enzyme's substrate specificity, crystal structures of YgjG from Escherichia coli were determined at 2.3 and 2.1 Å resolutions for the free and putrescine-bound enz… Show more

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Cited by 20 publications
(21 citation statements)
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“…[21] The highest activity was observed with putrescine (1c,s et to 100 %), and thereafter,t he activity subsequently decreasedi nastepwise mannerw ith increasing chain length from 1d to 1f.D iamines containing greater than eight C atoms, that is, 1g-i,h ad correspondingly lower measureable activity.W ea lso examined diamines 2a-c, 3a,a nd 3b containing heteroatoms in addition to branched diamine 4.A ll of these diamines were shown to be active, although the lower activities of the bulky substrates can possibly be rationalized by the presence of as mall substrate binding-site entrance with ah ighlyh ydrophobic channel to the active-site cavity relative to that of other class III transaminases. [22] Interestingly,p utrescine transaminase was found to exhibit highers electivity for diamines than for monoamines of comparable size;f or example, putrescine (1c)s howedh igha ctivity with Ec-ygjG pATA,w hereas correspondingm onoamine butyl amine 6 showed no detectible activity. Ornithine 5,m ono Ntert-butoxycarbonyl (Boc)-protected derivatives of 1a and 1b (amines 10 and 11,r espectively), and diamines 7a, 7b, 8,a nd 9 were also found to be inactives ubstrates, which suggests that the ygjG enzyme is strictly involved in the degradation of linear diamines (see Ta ble S2).…”
mentioning
confidence: 99%
“…[21] The highest activity was observed with putrescine (1c,s et to 100 %), and thereafter,t he activity subsequently decreasedi nastepwise mannerw ith increasing chain length from 1d to 1f.D iamines containing greater than eight C atoms, that is, 1g-i,h ad correspondingly lower measureable activity.W ea lso examined diamines 2a-c, 3a,a nd 3b containing heteroatoms in addition to branched diamine 4.A ll of these diamines were shown to be active, although the lower activities of the bulky substrates can possibly be rationalized by the presence of as mall substrate binding-site entrance with ah ighlyh ydrophobic channel to the active-site cavity relative to that of other class III transaminases. [22] Interestingly,p utrescine transaminase was found to exhibit highers electivity for diamines than for monoamines of comparable size;f or example, putrescine (1c)s howedh igha ctivity with Ec-ygjG pATA,w hereas correspondingm onoamine butyl amine 6 showed no detectible activity. Ornithine 5,m ono Ntert-butoxycarbonyl (Boc)-protected derivatives of 1a and 1b (amines 10 and 11,r espectively), and diamines 7a, 7b, 8,a nd 9 were also found to be inactives ubstrates, which suggests that the ygjG enzyme is strictly involved in the degradation of linear diamines (see Ta ble S2).…”
mentioning
confidence: 99%
“…1-D). This is also true for other AT-II transaminases (such as DAPA-AT [59] and PUAT [68]) suggesting that these enzymes do not generally undergo closure of the active site as the AT-I enzymes do [57,69].…”
Section: The Substrate Binding Site: a Gateway System In α-Kg-specifimentioning
confidence: 84%
“…Compared to Arg, the Lys side chain is smaller and less basic (meaning that it can more easily exist in neutral form), and these differences may help explain the low activity of PUAT towards ornithine and other amino donors containing an α-carboxylate. Another difference noted by the authors of the structural paper relates to the active site entrance, which appears narrower and more restricted in PUAT, possibly favoring access of the 'leaner' polyamines (putrescine and cadaverine) with respect to the bulkier amino acids [68].…”
Section: The Substrate Binding Site: a Gateway System In α-Kg-specifimentioning
confidence: 91%
See 1 more Smart Citation
“…Crystallization of Y30F/Y55F/Y115F/D38N KSI complexed with equilenin was conducted using a hanging drop vapor diffusion method as described previously ( Cha et al, 2014 ; Cho et al, 1999 ). After 20 mg/ml of the mutant KSI was prepared in a buffer containing 40 mM potassium phosphate, pH 7.0, 1 mM EDTA, and 20 mM β-mercaptoethanol, the 70 μl of this solution was mixed with 2 μl of 10 mM equilenin in dimethyl sulfoxide.…”
Section: Methodsmentioning
confidence: 99%