FERMENTATION OF ORNITHINE BY CLOSTRIDIUM STICKLANDII
FERMENTATION OF ORNITHINE BY CLOSTRIDIUM STICKLANDII
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DOI：
10.1128/jb.96.5.1617-1622.1968
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发表时间：
1968-01-01
影响因子：
3.2
通讯作者：
COSTILOW, RN
中科院分区：
文献类型：
--
作者：
DYER, JK;COSTILOW, RN
粘性梭菌的静息细胞通过以脯氨酸作为电子受体的耦合氧化还原作用以l-鸟氨酸作为单一底物进行发酵。鸟氨酸单独发酵的产物按浓度顺序依次为氨、丙氨酸、乙酸盐和δ-氨基戊酸。还发现了痕量的二氧化碳、丁酸盐和脯氨酸。当等摩尔量的脯氨酸与鸟氨酸一起添加时，鸟氨酸产生很少的δ-氨基戊酸，但基本上所有脯氨酸都被还原成该化合物。其他初级产物的比例因脯氨酸的添加而改变。在脯氨酸存在下发酵的鸟氨酸的主要产物是乙酸盐、氨、丙氨酸和二氧化碳，按浓度顺序排列。对 dl-鸟氨酸-1-14C、dl-鸟氨酸-2-14C 和 dl-鸟氨酸-5-14C 的研究表明，该氨基酸的初级裂解发生在碳 3 和 4 之间。来自碳 1 和 2 的同位素在丙氨酸中发现了很高的比例，而大部分来自碳 5 的同位素在挥发酸中发现。形成的CO2源自羧基碳。 dl-丙氨酸-1-14C发酵产生的所有放射性均在 14CO2 中发现。鸟氨酸中的丙氨酸被d-氨基酸氧化酶氧化至与dl-丙氨酸相同的程度，表明它是dl-α-丙氨酸。细胞提取物的初步实验表明脯氨酸是鸟氨酸还原成δ-氨基戊酸的中间体。
Resting cells ofClostridium sticklandiifermentedl-ornithine as a single substrate by a coupled oxidation-reduction with proline as the electron acceptor. The products of the fermentation of ornithine alone were ammonia, alanine, acetate, and δ-aminovalerate, in order of concentration. Traces of CO2, butyrate, and proline were also found. When an equimolar amount of proline was added along with ornithine, very little δ-aminovalerate was produced from the ornithine, but essentially all of the proline was reduced to this compound. The ratios of the other primary products were changed by the addition of proline. The primary products from ornithine fermented in the presence of proline were acetate, ammonia, alanine, and CO2, in order of concentration. Studies withdl-ornithine-1-14C,dl-ornithine-2-14C, anddl-ornithine-5-14Cdemonstrated that the primary cleavage of this amino acid occurred between carbons 3 and 4. A high percentage of the isotope from carbons 1 and 2 was found in alanine, and most of that from carbon 5 was found in volatile acid. The CO2formed was derived from the carboxyl carbon. All of the radioactivity from the fermentation ofdl-alanine-1-14Cwas found in14CO2. The alanine from ornithine was oxidized byd-amino acid oxidase to the same extent asdl-alanine, indicating that it wasdl-α-alanine. Preliminary experiments with cell extracts indicated proline is an intermediate in the reduction of ornithine to δ-aminovaleric acid.