Aldehyde Dehydrogenase Gene Superfamily Research Articles

Genome-Wide Characterization of the Aldehyde Dehydrogenase Gene Superfamily in Maize and Its Potential Role in Anther Development

Genome-Wide Characterization of the Aldehyde Dehydrogenase Gene Superfamily in Maize and Its Potential Role in Anther Development

Genome-wide characterization and gene expression analyses of ALDH gene family in response to drought stress in moso bamboo (Phyllostachys edulis)

Aldehyde dehydrogenase (ALDH) superfamily, comprising enzymes dependent on NAD+ or NADP+, plays an important role in controlling plant growth and development, as well as in responsing to phytohormone and environmental stress. These enzymes possess the ability to prevent toxic effects of aldehydes by converting them into their corresponding carboxylic acids. However, the potential function of ALDH genes in moso bamboo (Phyllostachys edulis) remains largely unknown. In this study, the ALDH gene superfamily in moso bamboo was analyzed through genome-wide screening, the evolutionary relationship of expansion genes was conducted. Tissue-specific expression patterns of ALDH genes were observed in 26 different tissues. Plant hormone and environmental stress responsive cis-elements were identified in the promoter of ALDH genes, which were supported by public databases data on the expression patterns under various abiotic stresses and hormone treatments. ALDH activity was increased in moso bamboo seedlings exposed to drought, compared to control condition. Furthermore, PeALDH2B2 was found to physically interact with PeGPB1 in response to drought. Overall, the study provides a comprehensive analysis of the ALDH family in moso bamboo and contributes to our understanding of the function of ALDH genes in growth, development, and adaptation to drought stresses.

Comparative genomic analysis of the aldehyde dehydrogenase gene superfamily in Arabidopsis thaliana - searching for the functional key to hypoxia tolerance.

Flooding entails different stressful conditions leading to low oxygen availability for respiration and as a result plants experience hypoxia. Stress imposed by hypoxia affects cellular metabolism, including the formation of toxic metabolites that dramatically reduce crop productivity. Aldehyde dehydrogenases (ALDHs) are a group of enzymes participating in various aspects of plant growth, development and stress responses. Although we have knowledge concerning the multiple functionalities of ALDHs in tolerance to various stresses, the engagement of ALDH in plant metabolism adjustment to hypoxia is poorly recognized. Therefore, we explored the ALDH gene superfamily in the model plant Arabidopsis thaliana. Genome-wide analyses revealed that 16 AtALDH genes are organized into ten families and distributed irregularly across Arabidopsis 5 chromosomes. According to evolutionary relationship studies from different plant species, the ALDH gene superfamily is highly conserved. AtALDH2 and ALDH3 are the most numerous families in plants, while ALDH18 was found to be the most distantly related. The analysis of cis-acting elements in promoters of AtALDHs indicated that AtALDHs participate in responses to light, phytohormones and abiotic stresses. Expression profile analysis derived from qRT-PCR showed the AtALDH2B7, AtALDH3H1 and AtALDH5F1 genes as the most responsive to hypoxia stress. In addition, the expression of AtALDH18B1, AtALDH18B2, AtALDH2B4, and AtALDH10A8 was highly altered during the post-hypoxia-reoxygenation phase. Taken together, we provide comprehensive functional information on the ALDH gene superfamily in Arabidopsis during hypoxia stress and highlight ALDHs as a functional element of hypoxic systemic responses. These findings might help develop a framework for application in the genetic improvement of crop plants.

New Aspects in the Mechanism of Action of ALDH1A1 and 1A3 Isoforms in Carcinogenesis

The ALDH gene superfamily encodes a group of evolutionarily-related proteins catalyzing the irreversible oxidation of aldehyde substrates to their corresponding carboxylic acids. Aldehyde dehydrogenases (ALDH) isoforms 1A1 and 1A3 belong to intracellular enzymes with a broad spectrum of functions linked with an advanced stage of solid tumors and the stemness potential of the neoplastic cells.

A comprehensive survey of the aldehyde dehydrogenase gene superfamily in Saccharum and the role of ScALDH2B-1 in the stress response

Aldehyde dehydrogenases (ALDHs) belong to NAD(P) + -dependent enzymes and are considered ‘‘aldehyde scavengers’’. They play crucial roles in growth, development, and environmental stress adaptation in plants. In this study, a total of 70 SsALDH and 14 ShALDH superfamily genes were identified in Saccharum spontaneum and Saccharum spp. R570 cultivar, respectively. Results showed that the SsALDH superfamily was classified into 10 ALDH families, and the ShALDH superfamily was divided into eight ALDH families. A co-expression network analysis suggested that these ALDH proteins may play vital roles in the stress response due to the fact that they are involved in the metabolism of proline, γ-aminobutyrate, and lysine. The promotor cis- element prediction revealed that the ALDH genes may be regulated by many phytohormones and are involved in various stress responses. RNA-seq data and qRT-PCR analysis inferred that ALDH genes in Saccharum played various roles in response to drought, cold and Sporisorium scitamineum stresses, and they were constitutively expressed in different sugarcane tissues. Additionally, an expression analysis of ScALDH2B-1 suggested significant changes under various stresses. The prokaryotic expression of ScALDH2B-1 in Escherichia coli BL21 cells resulted in enhanced tolerance to salinity. The ectopic expression of ScALDH2B-1 in Nicotiana benthamiana showed that, after challenged by Fusarium solani var. coeruleum, several HR maker genes were upregulated, while the accumulation of H 2 O 2 and HR-like cell death were triggered. A working model of the function of ALDHs in the Saccharum species was thus proposed. This study contributes to our understanding of the evolution and function of ALDH superfamily genes in Saccharum , and it also provides a baseline for the function identification of ScALDH2B-1 under biotic stress. • Totally, 70 SsALDH and 14 ShALDH were identified in Saccharum spontaneum and Saccharum spp. R570 cultivar, respectively. • SsALDH superfamily was classified into ten ALDH families and ShALDH superfamily was divided into eight ALDH families. • Co-expression network indicated that ALDH proteins involved in the metabolism of proline, γ-aminobutyrate, and lysine. • Promotor cis -element and expression profiles analysis suggested that ALDHs may play vital roles under various stresses. • The function analysis of ScALDH2B-1 showed it might play an important role under various abiotic and biotic stimuli.

Genome-wide characterization of the aldehyde dehydrogenase gene superfamily in soybean and its potential role in drought stress response

BackgroundAldehyde dehydrogenases (ALDHs) represent a group of enzymes that detoxify aldehydes by facilitating their oxidation to carboxylic acids, and have been shown to play roles in plant response to abiotic stresses. However, the comprehensive analysis of ALDH superfamily in soybean (Glycine max) has been limited.ResultsIn present study, a total of 53 GmALDHs were identified in soybean, and grouped into 10 ALDH families according to the ALDH Gene Nomenclature Committee and phylogenetic analysis. These groupings were supported by their gene structures and conserved motifs. Soybean ALDH superfamily expanded mainly by whole genome duplication/segmental duplications. Gene network analysis identified 1146 putative co-functional genes of 51 GmALDHs. Gene Ontology (GO) enrichment analysis suggested the co-functional genes of these 51 GmALDHs were enriched (FDR < 1e-3) in the process of lipid metabolism, photosynthesis, proline catabolism, and small molecule catabolism. In addition, 22 co-functional genes of GmALDHs are related to plant response to water deprivation/water transport. GmALDHs exhibited various expression patterns in different soybean tissues. The expression levels of 13 GmALDHs were significantly up-regulated and 14 down-regulated in response to water deficit. The occurrence frequencies of three drought-responsive cis-elements (ABRE, CRT/DRE, and GTGCnTGC/G) were compared in GmALDH genes that were up-, down-, or non-regulated by water deficit. Higher frequency of these three cis-elements was observed for the group of up-regulated GmALDH genes as compared to the group of down- or non- regulated GmALDHs by drought stress, implying their potential roles in the regulation of soybean response to drought stress.ConclusionsA total of 53 ALDH genes were identified in soybean genome and their phylogenetic relationships and duplication patterns were analyzed. The potential functions of GmALDHs were predicted by analyses of their co-functional gene networks, gene expression profiles, and cis-regulatory elements. Three GmALDH genes, including GmALDH3H2, GmALDH12A2 and GmALDH18B3, were highly induced by drought stress in soybean leaves. Our study provides a foundation for future investigations of GmALDH gene function in soybean.

Comparative genomic study of ALDH gene superfamily in Gossypium: A focus on Gossypium hirsutum under salt stress.

Aldehyde dehydrogenases (ALDHs) are a superfamily of enzymes which play important role in the scavenging of active aldehydes molecules. In present work, a comprehensive whole-genomic study of ALDH gene superfamily was carried out for an allotetraploid cultivated cotton species, G. hirsutum, as well as in parallel relative to their diploid progenitors, G. arboreum and G. raimondii. Totally, 30 and 58 ALDH gene sequences belong to 10 families were identified from diploid and allotetraploid cotton species, respectively. The gene structures among the members from same families were highly conserved. Whole-genome duplication and segmental duplication might be the major driver for the expansion of ALDH gene superfamily in G. hirsutum. In addition, the expression patterns of GhALDH genes were diverse across tissues. Most GhALDH genes were induced or repressed by salt stress in upland cotton. Our observation shed lights on the molecular evolutionary properties of ALDH genes in diploid cottons and their alloallotetraploid derivatives. It may be useful to mine key genes for improvement of cotton response to salt stress.

Genome-Wide Identification and Functional Classification of Tomato (Solanum lycopersicum) Aldehyde Dehydrogenase (ALDH) Gene Superfamily

Aldehyde dehydrogenases (ALDHs) is a protein superfamily that catalyzes the oxidation of aldehyde molecules into their corresponding non-toxic carboxylic acids, and responding to different environmental stresses, offering promising genetic approaches for improving plant adaptation. The aim of the current study is the functional analysis for systematic identification of S. lycopersicum ALDH gene superfamily. We performed genome-based ALDH genes identification and functional classification, phylogenetic relationship, structure and catalytic domains analysis, and microarray based gene expression. Twenty nine unique tomato ALDH sequences encoding 11 ALDH families were identified, including a unique member of the family 19 ALDH. Phylogenetic analysis revealed 13 groups, with a conserved relationship among ALDH families. Functional structure analysis of ALDH2 showed a catalytic mechanism involving Cys-Glu couple. However, the analysis of ALDH3 showed no functional gene duplication or potential neo-functionalities. Gene expression analysis reveals that particular ALDH genes might respond to wounding stress increasing the expression as ALDH2B7. Overall, this study reveals the complexity of S. lycopersicum ALDH gene superfamily and offers new insights into the structure-functional features and evolution of ALDH gene families in vascular plants. The functional characterization of ALDHs is valuable and promoting molecular breeding in tomato for the improvement of stress tolerance and signaling.

Aldehyde Dehydrogenase Gene Superfamily in Populus: Organization and Expression Divergence between Paralogous Gene Pairs.

Aldehyde dehydrogenases (ALDHs) constitute a superfamily of NAD(P)+-dependent enzymes that catalyze the irreversible oxidation of a wide range of reactive aldehydes to their corresponding nontoxic carboxylic acids. ALDHs have been studied in many organisms from bacteria to mammals; however, no systematic analyses incorporating genome organization, gene structure, expression profiles, and cis-acting elements have been conducted in the model tree species Populus trichocarpa thus far. In this study, a comprehensive analysis of the Populus ALDH gene superfamily was performed. A total of 26 Populus ALDH genes were found to be distributed across 12 chromosomes. Genomic organization analysis indicated that purifying selection may have played a pivotal role in the retention and maintenance of PtALDH gene families. The exon-intron organizations of PtALDHs were highly conserved within the same family, suggesting that the members of the same family also may have conserved functionalities. Microarray data and qRT-PCR analysis indicated that most PtALDHs had distinct tissue-specific expression patterns. The specificity of cis-acting elements in the promoter regions of the PtALDHs and the divergence of expression patterns between nine paralogous PtALDH gene pairs suggested that gene duplications may have freed the duplicate genes from the functional constraints. The expression levels of some ALDHs were up- or down-regulated by various abiotic stresses, implying that the products of these genes may be involved in the adaptation of Populus to abiotic stresses. Overall, the data obtained from our investigation contribute to a better understanding of the complexity of the Populus ALDH gene superfamily and provide insights into the function and evolution of ALDH gene families in vascular plants.

Single amino acid polymorphism in aldehyde dehydrogenase gene superfamily.

The aldehyde dehydrogenase gene superfamily comprises of 19 genes and 3 pseudogenes. These superfamily genes play a vital role in the formation of molecules that are involved in life processes, and detoxification of endogenous and exogenous aldehydes. ALDH superfamily genes associated mutations are implicated in various diseases, such as pyridoxine-dependent seizures, gamma-hydroxybutyric aciduria, type II Hyperprolinemia, Sjogren-Larsson syndrome including cancer and Alzheimer's disease. Accumulation of large DNA variations data especially Single Amino acid Polymorphisms (SAPs) in public databases related to ALDH superfamily genes insisted us to conduct a survey on the disease associated mutations and predict their function impact on protein structure and function. Overall this study provides an update and highlights the importance of pathogenic mutations in associated diseases. Using KD4v and Project HOPE a computational based platform, we summarized all the deleterious properties of SAPs in ALDH superfamily genes by the providing valuable insight into structural alteration rendered due to mutation. We hope this review might provide a way to define the deleteriousness of a SAP and helps to understand the molecular basis of the associated disease and also permits precise diagnosis and treatment in the near future.

The soybean aldehyde dehydrogenase (ALDH) protein superfamily

Aldehyde dehydrogenases (ALDHs) are members of NAD(P)+-dependent protein superfamily that catalyze the oxidation of a wide range of endogenous and exogenous highly reactive aliphatic and aromatic aldehyde molecules to their corresponding non toxic carboxylic acids. Research evidence has shown that ALDHs represent a promising class of genes to improve growth development, seed storage and environmental stress adaptation in higher plants. The recently completed genome sequences of several plant species have resulted in the identification of a large number of ALDH genes, most of which still need to be functionally characterized. In this paper, we identify members of the ALDH gene superfamily in soybean genome, and provide a unified nomenclature for the entire soybean ALDH gene families. The soybean genome contains 18 unique ALDH sequences encoding members of five ALDH families involved in a wide range of metabolic and molecular detoxification pathways. In addition, we describe the biochemical requirements and cellular metabolic pathways of selected members of ALDHs in soybean responses to environmental stress conditions.

Molecular cloning of a stress-responsive aldehyde dehydrogenase gene ScALDH21 from the desiccation-tolerant moss Syntrichia caninervis and its responses to different stresses

Aldehyde dehydrogenases (ALDHs) are key enzymes of abiotic stress-tolerance in a variety of organisms. The ALDH gene superfamily in eukaryotes has identified 22 protein families based upon sequence identity. ALDH21 is unique to mosses and represented by a single transcript gene in the desiccation-tolerant moss Tortula ruralis. We describe the cloning and characterization of an ALDH21 homologue from Syntrichia caninervis (ScALDH21), an extremely desiccation-tolerant moss found in deserts of Central Asia. The ScALDH21 cDNA is 1,452 bp and encodes a deduced polypeptide of 483 amino acids (53 kDa), approximately 97% identical to T. ruralis ALDH21 (TrALDH21A). The ScALDH21 gene was subcloned into pET26b(+) and expressed in Escherichia coli (Rosetta) to determine the peptides function in response to desiccation and salinity. Quantitative RT-PCR was used to analyze steady-state mRNA amounts in response to Abscisic acid (ABA) and desiccation. ScALDH21 transcript levels increased significantly in response to both desiccation and ABA. In the transgenic E. coli, ScALDH21 protein could be induced under the salinity and desiccation stress and was more abundant within salt-treated gametophores relative to control tissue. The data suggest that ScALDH21 participates in the stress-resistant pathways and plays an important role in response to desiccation and salinity stresses.

Modeling-dependent protein characterization of the rice aldehyde dehydrogenase (ALDH) superfamily reveals distinct functional and structural features.

The completion of the rice genome sequence has made it possible to identify and characterize new genes and to perform comparative genomics studies across taxa. The aldehyde dehydrogenase (ALDH) gene superfamily encoding for NAD(P)+-dependent enzymes is found in all major plant and animal taxa. However, the characterization of plant ALDHs has lagged behind their animal- and prokaryotic-ALDH homologs. In plants, ALDHs are involved in abiotic stress tolerance, male sterility restoration, embryo development and seed viability and maturation. However, there is still no structural property-dependent functional characterization of ALDH protein superfamily in plants. In this paper, we identify members of the rice ALDH gene superfamily and use the evolutionary nesting events of retrotransposons and protein-modeling–based structural reconstitution to report the genetic and molecular and structural features of each member of the rice ALDH superfamily in abiotic/biotic stress responses and developmental processes. Our results indicate that rice-ALDHs are the most expanded plant ALDHs ever characterized. This work represents the first report of specific structural features mediating functionality of the whole families of ALDHs in an organism ever characterized.

The aldehyde dehydrogenase (ALDH) gene superfamily of the moss Physcomitrella patens and the algae Chlamydomonas reinhardtii and Ostreococcus tauri

The assembled Physcomitrella patens genome has been released. This provides a unique opportunity to identify and characterize new genes, and to compare moss genes with other plant genes from previously released plant genomes. Aldehyde dehydrogenases (ALDHs) comprise a protein superfamily of NAD(P) -dependent enzymes [EC 1.2.1] found in bacteria, animals and green plants capable of oxidizing a variety of aromatic and aliphatic aldehydes. ALDHs are key enzymes of abiotic stress-tolerance in a variety of organisms. In bryophytes, ALDHs are postulated to play a role in vegetative desiccation-tolerance. Using recently available genomic DNA sequence data, we have identified members of the ALDH gene superfamily in the marine picoeukaryote Ostreococcus tauri, the unicellular green algae Chlamydomonas reinhardtii and the moss Physcomitrella patens. The Arabidopsis thaliana genome has been shown to contain 14 unique ALDH sequences encoding members of nine ALDH protein families. The O. tauri genome contains six unique ALDH sequences encoding members of six ALDH protein families. The C. reinhardtii genome contains eight unique ALDH sequences encoding members of seven ALDH protein families. The P. patens genome contains 20 unique ALDH sequences encoding members of ten ALDH protein families. These three genomes encode members of ten previously identified protein families (ALDH2, ALDH3, ALDH5, ALDH6, ALDH7, ALDH10, ALDH11, ALDH12, ALDH21 and ALDH22) and two novel protein families (ALDH23 and ALDH24). We analyzed a sequence alignment of ALDH deduced amino acid sequences among plants using neighbor-joining and maximum parsimony methods. These analyses demonstrate that 1) at least eight ALDH protein families, as represented in the O. tauri and/or C. reinhardtii genomes were present prior to the evolution of land plants and each of these families have been maintained throughout land plant evolution, 2) novel ALDH families of as yet unknown function have evolved in several lineages of land plants including the mosses and flowering plants and 3) the moss P. patens exhibits a highly expanded set of sequences in three families, ALDH3, ALDH5 and ALDH11.

The Aldehyde Dehydrogenase Gene Superfamily Resource Center

The website http://www.aldh.org is a publicly available database for nomenclature and functional and molecular sequence information for members of the aldehyde dehydrogenase (ALDH) gene superfamily for animals, plants, fungi and bacteria. The site has organised gene-specific records. It provides synopses of ALDH gene records, marries trivial terms to correct nomenclature and links global accession identifiers with source data. Server-side alignment software characterises the integrity of each sequence relative to the latest genomic assembly and provides identifier-specific detail reports, including a graphical presentation of the transcript's exon - intron structure, its size, coding sequence, genomic strand and locus. Also included are a summary of substrates, inhibitors and enzyme kinetics. The site provides reference lists and is designed to facilitate data mining by interested investigators.

Analysis and update of the human aldehyde dehydrogenase (ALDH) gene family

The aldehyde dehydrogenase (ALDH) gene superfamily encodes enzymes that are critical for certain life processes and detoxification via the NAD(P)+-dependent oxidation of numerous endogenous and exogenous aldehyde substrates, including pharmaceuticals and environmental pollutants. Analysis of the ALDH gene superfamily in the latest databases showed that the human genome contains 19 putatively functional genes and three pseudogenes. A number of ALDH genes are upregulated as a part of the oxidative stress response and inexplicably overexpressed in various tumours, leading to problems during cancer chemotherapy. Mutations in ALDH genes cause inborn errors of metabolism -- such as the Sjögren - Larsson syndrome, type II hyperprolinaemia and γ-hydroxybutyric aciduria -- and are likely to contribute to several complex diseases, including cancer and Alzheimer's disease. The ALDH gene products appear to be multifunctional proteins, possessing both catalytic and non-catalytic properties.

The ALDH gene superfamily of Arabidopsis

Aldehyde dehydrogenases (ALDHs) represent a protein superfamily of NAD(P)(+)-dependent enzymes that oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes. The Arabidopsis genome contains 14 unique ALDH sequences encoding members of nine ALDH families, including eight known families and one novel family (ALDH22) that is currently known only in plants. Here, we identify members of the ALDH gene superfamily in Arabidopsis; provide a revised, unified nomenclature for these ALDH genes; analyze the molecular relationship among Arabidopsis ALDH genes and compare them to ALDH genes from other species, including prokaryotes and mammals; and describe the role of ALDHs in cytoplasmic male sterility, plant defense and abiotic stress tolerance.

Aldehyde dehydrogenase gene superfamily: the 2002 update

The aldehyde dehydrogenase (ALDH) superfamily represents a divergently related group of enzymes that metabolize a wide variety of endogenous and exogenous aldehydes. With the advent of megabase genome sequencing, the ALDH superfamily is continuously expanding on many fronts. The presence of ALDH encoding genes in the vast majority of archaeal, eubacterial and eukaryotic genomes supports the notion that these enzymes are important components of metabolic processes in living organisms and that the ALDH superfamily is ancient in origin. As of July 2002, the ALDH superfamily consists of 555 distinct genes: 32 in archaea, 351 in eubacteria, and 172 in eukaryota. Complete sequencing of individual genomes reveals the number of ALDH genes found per organism ranges from 1 to 5 in archaeal species, 1–26 genes in eubacterial species, and 8–17 genes in eukaryotic species. In the human genome, 17 functional genes and 3 pseudogenes have been identified to date. A standardized ALDH gene nomenclature system has been developed based on multiple alignment analysis of eukaryotic ALDH amino acid sequences. Both Human and Mouse Genome Projects have accepted this nomenclature system. In this report, we present a complete listing of all ALDH sequences known to date, along with the evolutionary analysis of the eukaryotic ALDHs. Thus far, the eukaryotic ALDHs comprise 20 gene families. Detailed information on ALDH gene superfamily is also available at http://www.uchsc.edu/sp/sp/alcdbase/aldhcov.html.

Aldehyde dehydrogenase gene superfamily: the 2000 update

Aldehyde dehydrogenase (ALDH) superfamily represents a group of NAD(P) +-dependent enzymes that catalyze the oxidation of a wide spectrum of endogenous and exogenous aldehydes. With the advent of megabase genome sequencing, the ALDH superfamily is expanding rapidly on many fronts. As expected, ALDH genes are found in virtually all genomes analyzed to date, indicating the importance of these enzymes in biological functions. Complete genome sequences of various species have revealed additional ALDH genes. As of July 2000, the ALDH superfamily consists of 331 distinct genes, of which eight are found in archaea, 165 in eubacteria, and 158 in eukaryota. The number of ALDH genes in some species with their genomes completely sequenced and annotated, Escherichia coli and Caenorhabditis elegans, ranges from 10 to 17. In the human genome, 17 functional genes and three pseudogenes have been identified to date. Divergent evolution, based on multiple alignment analysis of 86 eukaryotic ALDH amino-acid sequences, was the basis of the standardized ALDH gene nomenclature system (Pharmacogenetics 9: 421–434, 1999). Thus far, the eukaryotic ALDHs comprise 20 gene families. A complete list of all ALDH sequences known to date is presented here along with the evolution analysis of the eukaryotic ALDHs.

Aldehyde dehydrogenase gene superfamily. The 1998 update.

Aldehydehydrogenases (ALDHs) represent a group of NAD(P)+-dependent enzymes, which e similar primary structures and oxidize a wide spectrum of endogenous and exnous aldehydes (Lindahl, 1992; Vasiliou et al., 1995). Several ALDHs display broad strate specificities, oxidizing a variety of both aliphatic and aromatic aldehydes, whereather forms possess narrower substrate preferences. Based on substrate specificities, ALDH emes are broadly categorized as:a. semialdehyde dehydrogenases, including hydroxymuconic semialdehyde dehydrogenase (E.C. 1.2.1.32), Escherichia coli (EC 1.2.1.16) and mammalian (EC 1.2.1.24) succinate-semialdehyde dehydrogenase, glutamate semi aldehyde dehydrogenase (E.C. 1.2.1.41), aspartate semialdehyde dehydrogenase (E.C. 1.2.1.11), 2-amino-adipate-6-semialdehyde dehydrogenase (E.C. 1.2.1.31) and metylmalonate- semialdehyde dehydrogenase (E.C. 1.2.1.27), b. nonspecific ALDHs (E.C.I.2.1.3), c. other ALDHs including betaine dehydrogenase (E.C. 1.2.1.8), non phosphorylating glyceraldehyde 3-phosphatedehydrogenase (E.C. 1.2.1.9), phenylacetaldehyde dehydrogenase (EC 1.2.1.39), lactaldehyde dehydrogenase (EC 1.2.1.22), and d. ALDike proteins which represent certain other protein sequences, containing either complete or almost complete ALDH sequences. These include the 10-formyltetrahydrofolate dehydrogenase (E.C. 1.5.1.6), Δ1-pyrroline-5-carboxylate dehydrogenase (EC 1.5.1.12), antiquitin, a human 56-kDa androgen-binding protein, and the crystallins..KeywordsBacillus SubtilisAromatic AldehydeClostridium AcetobutylicumGene SuperfamilyDeinococcus RadioduransThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.