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乙酸激酶:不仅仅是一种细菌酶。

Acetate kinase: not just a bacterial enzyme.

作者信息

Ingram-Smith Cheryl, Martin Stephen R, Smith Kerry S

机构信息

Department of Genetics and Biochemistry, Clemson University, Clemson, SC 29634-0318, USA.

出版信息

Trends Microbiol. 2006 Jun;14(6):249-53. doi: 10.1016/j.tim.2006.04.001. Epub 2006 May 4.

Abstract

The bacterial enzymes acetate kinase (AK) and phosphotransacetylase (PTA) form a key pathway for synthesis of the central metabolic intermediate acetyl coenzyme A (acetyl-CoA) from acetate or for generation of ATP from excess acetyl-CoA. Putative AK genes have now been identified in some eukaryotic microbes. In Chlamydomonas reinhardtii and Phytophthora species, AK forms a pathway with PTA. AK has also been identified in non-yeast fungi but these fungi do not have PTA. Instead, AK forms a pathway with D-xylulose 5-phosphate phosphoketolase (XFP), a pathway that was also previously found only in bacteria. In Entamoeba histolytica, neither PTA nor XFP was found as a partner for AK. Thus, eukaryotic microbes seem to have incorporated the 'bacterial' enzyme AK into at least three different metabolic pathways.

摘要

细菌酶乙酸激酶(AK)和磷酸转乙酰酶(PTA)构成了一条关键途径,可用于从乙酸盐合成中心代谢中间体乙酰辅酶A(乙酰辅酶A),或从过量的乙酰辅酶A生成ATP。现在已经在一些真核微生物中鉴定出了假定的AK基因。在莱茵衣藻和疫霉属物种中,AK与PTA形成一条途径。在非酵母真菌中也发现了AK,但这些真菌没有PTA。相反,AK与D-木酮糖5-磷酸磷酸酮醇酶(XFP)形成一条途径,该途径以前也仅在细菌中发现。在溶组织内阿米巴中,未发现PTA和XFP作为AK的伙伴。因此,真核微生物似乎已将“细菌”酶AK纳入至少三种不同的代谢途径中。

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